data_7HHI
# 
_entry.id   7HHI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HHI         pdb_00007hhi 10.2210/pdb7hhi/pdb 
WWPDB D_1001407480 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HHI 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '~{N},~{N}-dimethyl-1~{H}-pyrazole-4-sulfonamide'  175.209   1   ? ?    ? ? 
5 water       nat water                                              18.015    259 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                     SO4   
3 1,2-ETHANEDIOL                                    EDO   
4 '~{N},~{N}-dimethyl-1~{H}-pyrazole-4-sulfonamide' A1H9V 
5 water                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H9V non-polymer         . '~{N},~{N}-dimethyl-1~{H}-pyrazole-4-sulfonamide' N,N-dimethyl-1H-pyrazole-4-sulfonamide 
'C5 H9 N3 O2 S'  175.209 
ALA   'L-peptide linking' y ALANINE                                           ?                                      'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                          ?                                      
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                        ?                                      'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                   ?                                      'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                          ?                                      
'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                    'ETHYLENE GLYCOL'                      'C2 H6 O2' 
62.068  
GLN   'L-peptide linking' y GLUTAMINE                                         ?                                      
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                   ?                                      'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                           ?                                      'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                         ?                                      
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                             ?                                      'H2 O' 18.015 
ILE   'L-peptide linking' y ISOLEUCINE                                        ?                                      'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                           ?                                      'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                            ?                                      
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                        ?                                      
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                     ?                                      'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                           ?                                      'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                            ?                                      'C3 H7 N O3' 
105.093 
SO4   non-polymer         . 'SULFATE ION'                                     ?                                      'O4 S -2' 
96.063  
THR   'L-peptide linking' y THREONINE                                         ?                                      'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                        ?                                      
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                          ?                                      'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                            ?                                      'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 ?  ?   ?   B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H9V 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H9V 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4   1   101 95  SO4   SO4 A . 
E 2 SO4   1   102 96  SO4   SO4 A . 
F 3 EDO   1   103 97  EDO   EDO A . 
G 2 SO4   1   104 4   SO4   SO4 A . 
H 2 SO4   1   101 1   SO4   SO4 B . 
I 2 SO4   1   102 3   SO4   SO4 B . 
J 4 A1H9V 1   103 101 A1H9V LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 84  HOH   HOH A . 
M 5 HOH   2   202 109 HOH   HOH A . 
M 5 HOH   3   203 37  HOH   HOH A . 
M 5 HOH   4   204 349 HOH   HOH A . 
M 5 HOH   5   205 85  HOH   HOH A . 
M 5 HOH   6   206 333 HOH   HOH A . 
M 5 HOH   7   207 23  HOH   HOH A . 
M 5 HOH   8   208 139 HOH   HOH A . 
M 5 HOH   9   209 360 HOH   HOH A . 
M 5 HOH   10  210 202 HOH   HOH A . 
M 5 HOH   11  211 60  HOH   HOH A . 
M 5 HOH   12  212 274 HOH   HOH A . 
M 5 HOH   13  213 12  HOH   HOH A . 
M 5 HOH   14  214 87  HOH   HOH A . 
M 5 HOH   15  215 86  HOH   HOH A . 
M 5 HOH   16  216 32  HOH   HOH A . 
M 5 HOH   17  217 66  HOH   HOH A . 
M 5 HOH   18  218 342 HOH   HOH A . 
M 5 HOH   19  219 304 HOH   HOH A . 
M 5 HOH   20  220 288 HOH   HOH A . 
M 5 HOH   21  221 290 HOH   HOH A . 
M 5 HOH   22  222 116 HOH   HOH A . 
M 5 HOH   23  223 292 HOH   HOH A . 
M 5 HOH   24  224 151 HOH   HOH A . 
M 5 HOH   25  225 77  HOH   HOH A . 
M 5 HOH   26  226 301 HOH   HOH A . 
M 5 HOH   27  227 203 HOH   HOH A . 
M 5 HOH   28  228 71  HOH   HOH A . 
M 5 HOH   29  229 18  HOH   HOH A . 
M 5 HOH   30  230 94  HOH   HOH A . 
M 5 HOH   31  231 165 HOH   HOH A . 
M 5 HOH   32  232 97  HOH   HOH A . 
M 5 HOH   33  233 14  HOH   HOH A . 
M 5 HOH   34  234 111 HOH   HOH A . 
M 5 HOH   35  235 259 HOH   HOH A . 
M 5 HOH   36  236 164 HOH   HOH A . 
M 5 HOH   37  237 307 HOH   HOH A . 
M 5 HOH   38  238 28  HOH   HOH A . 
M 5 HOH   39  239 1   HOH   HOH A . 
M 5 HOH   40  240 190 HOH   HOH A . 
M 5 HOH   41  241 2   HOH   HOH A . 
M 5 HOH   42  242 188 HOH   HOH A . 
M 5 HOH   43  243 8   HOH   HOH A . 
M 5 HOH   44  244 278 HOH   HOH A . 
M 5 HOH   45  245 26  HOH   HOH A . 
M 5 HOH   46  246 91  HOH   HOH A . 
M 5 HOH   47  247 267 HOH   HOH A . 
M 5 HOH   48  248 99  HOH   HOH A . 
M 5 HOH   49  249 351 HOH   HOH A . 
M 5 HOH   50  250 300 HOH   HOH A . 
M 5 HOH   51  251 260 HOH   HOH A . 
M 5 HOH   52  252 115 HOH   HOH A . 
M 5 HOH   53  253 27  HOH   HOH A . 
M 5 HOH   54  254 31  HOH   HOH A . 
M 5 HOH   55  255 58  HOH   HOH A . 
M 5 HOH   56  256 7   HOH   HOH A . 
M 5 HOH   57  257 9   HOH   HOH A . 
M 5 HOH   58  258 95  HOH   HOH A . 
M 5 HOH   59  259 289 HOH   HOH A . 
M 5 HOH   60  260 34  HOH   HOH A . 
M 5 HOH   61  261 343 HOH   HOH A . 
M 5 HOH   62  262 293 HOH   HOH A . 
M 5 HOH   63  263 22  HOH   HOH A . 
M 5 HOH   64  264 55  HOH   HOH A . 
M 5 HOH   65  265 218 HOH   HOH A . 
M 5 HOH   66  266 47  HOH   HOH A . 
M 5 HOH   67  267 167 HOH   HOH A . 
M 5 HOH   68  268 78  HOH   HOH A . 
M 5 HOH   69  269 16  HOH   HOH A . 
M 5 HOH   70  270 143 HOH   HOH A . 
M 5 HOH   71  271 42  HOH   HOH A . 
M 5 HOH   72  272 281 HOH   HOH A . 
M 5 HOH   73  273 210 HOH   HOH A . 
M 5 HOH   74  274 179 HOH   HOH A . 
M 5 HOH   75  275 222 HOH   HOH A . 
M 5 HOH   76  276 206 HOH   HOH A . 
M 5 HOH   77  277 335 HOH   HOH A . 
M 5 HOH   78  278 63  HOH   HOH A . 
M 5 HOH   79  279 21  HOH   HOH A . 
M 5 HOH   80  280 40  HOH   HOH A . 
M 5 HOH   81  281 20  HOH   HOH A . 
M 5 HOH   82  282 83  HOH   HOH A . 
M 5 HOH   83  283 327 HOH   HOH A . 
M 5 HOH   84  284 131 HOH   HOH A . 
M 5 HOH   85  285 297 HOH   HOH A . 
M 5 HOH   86  286 64  HOH   HOH A . 
M 5 HOH   87  287 145 HOH   HOH A . 
M 5 HOH   88  288 113 HOH   HOH A . 
M 5 HOH   89  289 283 HOH   HOH A . 
M 5 HOH   90  290 171 HOH   HOH A . 
M 5 HOH   91  291 19  HOH   HOH A . 
M 5 HOH   92  292 73  HOH   HOH A . 
M 5 HOH   93  293 318 HOH   HOH A . 
M 5 HOH   94  294 219 HOH   HOH A . 
M 5 HOH   95  295 38  HOH   HOH A . 
M 5 HOH   96  296 75  HOH   HOH A . 
M 5 HOH   97  297 199 HOH   HOH A . 
M 5 HOH   98  298 205 HOH   HOH A . 
M 5 HOH   99  299 208 HOH   HOH A . 
M 5 HOH   100 300 156 HOH   HOH A . 
M 5 HOH   101 301 185 HOH   HOH A . 
M 5 HOH   102 302 211 HOH   HOH A . 
M 5 HOH   103 303 348 HOH   HOH A . 
M 5 HOH   104 304 152 HOH   HOH A . 
M 5 HOH   105 305 57  HOH   HOH A . 
M 5 HOH   106 306 35  HOH   HOH A . 
M 5 HOH   107 307 125 HOH   HOH A . 
M 5 HOH   108 308 332 HOH   HOH A . 
N 5 HOH   1   201 123 HOH   HOH B . 
N 5 HOH   2   202 69  HOH   HOH B . 
N 5 HOH   3   203 172 HOH   HOH B . 
N 5 HOH   4   204 258 HOH   HOH B . 
N 5 HOH   5   205 329 HOH   HOH B . 
N 5 HOH   6   206 247 HOH   HOH B . 
N 5 HOH   7   207 13  HOH   HOH B . 
N 5 HOH   8   208 119 HOH   HOH B . 
N 5 HOH   9   209 76  HOH   HOH B . 
N 5 HOH   10  210 17  HOH   HOH B . 
N 5 HOH   11  211 224 HOH   HOH B . 
N 5 HOH   12  212 302 HOH   HOH B . 
N 5 HOH   13  213 36  HOH   HOH B . 
N 5 HOH   14  214 169 HOH   HOH B . 
N 5 HOH   15  215 338 HOH   HOH B . 
N 5 HOH   16  216 117 HOH   HOH B . 
N 5 HOH   17  217 68  HOH   HOH B . 
N 5 HOH   18  218 98  HOH   HOH B . 
N 5 HOH   19  219 54  HOH   HOH B . 
N 5 HOH   20  220 153 HOH   HOH B . 
N 5 HOH   21  221 96  HOH   HOH B . 
N 5 HOH   22  222 346 HOH   HOH B . 
N 5 HOH   23  223 61  HOH   HOH B . 
N 5 HOH   24  224 6   HOH   HOH B . 
N 5 HOH   25  225 24  HOH   HOH B . 
N 5 HOH   26  226 168 HOH   HOH B . 
N 5 HOH   27  227 89  HOH   HOH B . 
N 5 HOH   28  228 261 HOH   HOH B . 
N 5 HOH   29  229 10  HOH   HOH B . 
N 5 HOH   30  230 316 HOH   HOH B . 
N 5 HOH   31  231 279 HOH   HOH B . 
N 5 HOH   32  232 320 HOH   HOH B . 
N 5 HOH   33  233 25  HOH   HOH B . 
N 5 HOH   34  234 160 HOH   HOH B . 
N 5 HOH   35  235 280 HOH   HOH B . 
N 5 HOH   36  236 303 HOH   HOH B . 
N 5 HOH   37  237 74  HOH   HOH B . 
N 5 HOH   38  238 44  HOH   HOH B . 
N 5 HOH   39  239 150 HOH   HOH B . 
N 5 HOH   40  240 175 HOH   HOH B . 
N 5 HOH   41  241 249 HOH   HOH B . 
N 5 HOH   42  242 214 HOH   HOH B . 
N 5 HOH   43  243 5   HOH   HOH B . 
N 5 HOH   44  244 201 HOH   HOH B . 
N 5 HOH   45  245 72  HOH   HOH B . 
N 5 HOH   46  246 341 HOH   HOH B . 
N 5 HOH   47  247 177 HOH   HOH B . 
N 5 HOH   48  248 59  HOH   HOH B . 
N 5 HOH   49  249 272 HOH   HOH B . 
N 5 HOH   50  250 170 HOH   HOH B . 
N 5 HOH   51  251 197 HOH   HOH B . 
N 5 HOH   52  252 315 HOH   HOH B . 
N 5 HOH   53  253 46  HOH   HOH B . 
N 5 HOH   54  254 101 HOH   HOH B . 
N 5 HOH   55  255 242 HOH   HOH B . 
N 5 HOH   56  256 120 HOH   HOH B . 
N 5 HOH   57  257 70  HOH   HOH B . 
N 5 HOH   58  258 163 HOH   HOH B . 
N 5 HOH   59  259 104 HOH   HOH B . 
N 5 HOH   60  260 291 HOH   HOH B . 
N 5 HOH   61  261 356 HOH   HOH B . 
N 5 HOH   62  262 217 HOH   HOH B . 
N 5 HOH   63  263 137 HOH   HOH B . 
N 5 HOH   64  264 223 HOH   HOH B . 
N 5 HOH   65  265 355 HOH   HOH B . 
N 5 HOH   66  266 92  HOH   HOH B . 
N 5 HOH   67  267 354 HOH   HOH B . 
N 5 HOH   68  268 322 HOH   HOH B . 
N 5 HOH   69  269 340 HOH   HOH B . 
N 5 HOH   70  270 79  HOH   HOH B . 
N 5 HOH   71  271 215 HOH   HOH B . 
N 5 HOH   72  272 182 HOH   HOH B . 
N 5 HOH   73  273 314 HOH   HOH B . 
N 5 HOH   74  274 336 HOH   HOH B . 
N 5 HOH   75  275 107 HOH   HOH B . 
N 5 HOH   76  276 312 HOH   HOH B . 
N 5 HOH   77  277 313 HOH   HOH B . 
N 5 HOH   78  278 359 HOH   HOH B . 
N 5 HOH   79  279 334 HOH   HOH B . 
N 5 HOH   80  280 339 HOH   HOH B . 
N 5 HOH   81  281 350 HOH   HOH B . 
O 5 HOH   1   201 317 HOH   HOH C . 
O 5 HOH   2   202 294 HOH   HOH C . 
O 5 HOH   3   203 209 HOH   HOH C . 
O 5 HOH   4   204 65  HOH   HOH C . 
O 5 HOH   5   205 254 HOH   HOH C . 
O 5 HOH   6   206 189 HOH   HOH C . 
O 5 HOH   7   207 226 HOH   HOH C . 
O 5 HOH   8   208 161 HOH   HOH C . 
O 5 HOH   9   209 295 HOH   HOH C . 
O 5 HOH   10  210 41  HOH   HOH C . 
O 5 HOH   11  211 118 HOH   HOH C . 
O 5 HOH   12  212 134 HOH   HOH C . 
O 5 HOH   13  213 15  HOH   HOH C . 
O 5 HOH   14  214 102 HOH   HOH C . 
O 5 HOH   15  215 184 HOH   HOH C . 
O 5 HOH   16  216 173 HOH   HOH C . 
O 5 HOH   17  217 135 HOH   HOH C . 
O 5 HOH   18  218 305 HOH   HOH C . 
O 5 HOH   19  219 122 HOH   HOH C . 
O 5 HOH   20  220 326 HOH   HOH C . 
O 5 HOH   21  221 4   HOH   HOH C . 
O 5 HOH   22  222 321 HOH   HOH C . 
O 5 HOH   23  223 142 HOH   HOH C . 
O 5 HOH   24  224 345 HOH   HOH C . 
O 5 HOH   25  225 45  HOH   HOH C . 
O 5 HOH   26  226 56  HOH   HOH C . 
O 5 HOH   27  227 90  HOH   HOH C . 
O 5 HOH   28  228 298 HOH   HOH C . 
O 5 HOH   29  229 108 HOH   HOH C . 
O 5 HOH   30  230 337 HOH   HOH C . 
O 5 HOH   31  231 53  HOH   HOH C . 
O 5 HOH   32  232 62  HOH   HOH C . 
O 5 HOH   33  233 275 HOH   HOH C . 
O 5 HOH   34  234 67  HOH   HOH C . 
O 5 HOH   35  235 299 HOH   HOH C . 
O 5 HOH   36  236 323 HOH   HOH C . 
O 5 HOH   37  237 146 HOH   HOH C . 
O 5 HOH   38  238 49  HOH   HOH C . 
O 5 HOH   39  239 269 HOH   HOH C . 
O 5 HOH   40  240 149 HOH   HOH C . 
O 5 HOH   41  241 82  HOH   HOH C . 
O 5 HOH   42  242 325 HOH   HOH C . 
O 5 HOH   43  243 344 HOH   HOH C . 
O 5 HOH   44  244 328 HOH   HOH C . 
O 5 HOH   45  245 296 HOH   HOH C . 
O 5 HOH   46  246 157 HOH   HOH C . 
O 5 HOH   47  247 48  HOH   HOH C . 
O 5 HOH   48  248 103 HOH   HOH C . 
O 5 HOH   49  249 198 HOH   HOH C . 
O 5 HOH   50  250 287 HOH   HOH C . 
O 5 HOH   51  251 309 HOH   HOH C . 
O 5 HOH   52  252 270 HOH   HOH C . 
O 5 HOH   53  253 319 HOH   HOH C . 
O 5 HOH   54  254 347 HOH   HOH C . 
O 5 HOH   55  255 126 HOH   HOH C . 
O 5 HOH   56  256 357 HOH   HOH C . 
O 5 HOH   57  257 241 HOH   HOH C . 
O 5 HOH   58  258 324 HOH   HOH C . 
O 5 HOH   59  259 284 HOH   HOH C . 
O 5 HOH   60  260 148 HOH   HOH C . 
O 5 HOH   61  261 130 HOH   HOH C . 
O 5 HOH   62  262 271 HOH   HOH C . 
O 5 HOH   63  263 361 HOH   HOH C . 
O 5 HOH   64  264 353 HOH   HOH C . 
O 5 HOH   65  265 330 HOH   HOH C . 
O 5 HOH   66  266 246 HOH   HOH C . 
O 5 HOH   67  267 358 HOH   HOH C . 
O 5 HOH   68  268 43  HOH   HOH C . 
O 5 HOH   69  269 352 HOH   HOH C . 
O 5 HOH   70  270 310 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
2  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
3  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
4  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
5  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
6  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
7  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
8  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
9  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
10 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
11 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
17 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
18 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
19 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
20 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
21 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
22 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
23 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
24 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
25 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
26 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
27 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
28 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
29 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
30 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
31 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
32 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
33 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
34 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
35 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
36 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
37 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
38 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
39 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
40 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
41 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
42 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
43 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
44 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
45 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
46 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
47 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
48 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
49 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
50 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
51 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
52 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
53 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
54 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
55 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
56 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
57 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
58 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
59 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
60 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
61 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
62 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHI 
_cell.length_a           41.416 
_cell.length_b           41.811 
_cell.length_c           157.693 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HHI 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.entry_id          7HHI 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.76 
_exptl_crystal.density_percent_sol   55.0 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '28% PEG MME 2000; 0.15 M ammonium sulfate; 0.1 M sodium acetate pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2021-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.918076 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.918076 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HHI 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             157.69 
_reflns.d_resolution_high            2.11 
_reflns.number_obs                   15980 
_reflns.percent_possible_obs         96.6 
_reflns.pdbx_Rmerge_I_obs            0.231 
_reflns.pdbx_netI_over_sigmaI        4.4 
_reflns.pdbx_redundancy              6.0 
_reflns.pdbx_Rrim_I_all              0.253 
_reflns.pdbx_Rpim_I_all              0.101 
_reflns.pdbx_CC_half                 0.984 
_reflns.pdbx_number_measured_all     96481 
_reflns.pdbx_chi_squared             0.95 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  2.11 
_reflns_shell.d_res_low                   2.22 
_reflns_shell.number_measured_all         13573 
_reflns_shell.number_unique_obs           2290 
_reflns_shell.Rmerge_I_obs                1.873 
_reflns_shell.pdbx_chi_squared            0.86 
_reflns_shell.pdbx_redundancy             5.9 
_reflns_shell.percent_possible_obs        98.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             2.049 
_reflns_shell.pdbx_Rpim_I_all             0.819 
_reflns_shell.pdbx_CC_half                0.536 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HHI 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     15080 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             78.85 
_refine.ls_d_res_high                            2.11 
_refine.ls_percent_reflns_obs                    96.25 
_refine.ls_R_factor_obs                          0.22784 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22171 
_refine.ls_R_factor_R_free                       0.33437 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  846 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.873 
_refine.B_iso_mean                               49.741 
_refine.aniso_B[1][1]                            -0.88 
_refine.aniso_B[2][2]                            -2.63 
_refine.aniso_B[3][3]                            3.51 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.329 
_refine.pdbx_overall_ESU_R_Free                  0.293 
_refine.overall_SU_ML                            0.318 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             13.097 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        2130 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             259 
_refine_hist.number_atoms_total               2438 
_refine_hist.d_res_high                       2.11 
_refine_hist.d_res_low                        78.85 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.006  0.012  ? 2280 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.655  1.834  ? 3103 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       9.218  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       7.423  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.105 10.000 ? 301  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.126  0.200  ? 288  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 1882 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  4.578  4.909  ? 1073 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.423  8.789  ? 1334 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.886  5.111  ? 1207 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       13.070 74.55  ? 3842 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.108 
_refine_ls_shell.d_res_low                        2.162 
_refine_ls_shell.number_reflns_R_work             1117 
_refine_ls_shell.R_factor_R_work                  0.378 
_refine_ls_shell.percent_reflns_obs               98.57 
_refine_ls_shell.R_factor_R_free                  0.420 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             53 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHI 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z805551440' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHI 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHI A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHI B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHI C 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HHI GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHI SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHI GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHI SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHI GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHI SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 50 ? LEU A 54 ? GLU A 49 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O LEU B 54 ? O LEU B 53 N TYR B 41 ? N TYR B 40 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HHI 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OD1 B ASP 26  ? ? O B HOH 201 ? ? 1.86 
2  1 O   B HOH 224 ? ? O B HOH 274 ? ? 2.00 
3  1 O   B HOH 235 ? ? O B HOH 268 ? ? 2.02 
4  1 OH  B TYR 40  ? ? O B HOH 202 ? ? 2.07 
5  1 O   A HOH 236 ? ? O A HOH 259 ? ? 2.09 
6  1 O   A PRO 37  ? ? O A HOH 201 ? ? 2.12 
7  1 O   B HOH 223 ? ? O B HOH 276 ? ? 2.13 
8  1 O   A PRO 7   ? ? O A HOH 202 ? ? 2.14 
9  1 O   B GLN 85  ? ? O B HOH 203 ? ? 2.14 
10 1 O   A HOH 273 ? ? O A HOH 275 ? ? 2.16 
11 1 O   A HOH 227 ? ? O A HOH 265 ? ? 2.18 
12 1 OD2 B ASP 26  ? ? O B HOH 204 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     220 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     262 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              2.06 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 36 ? ? -47.26  158.60 
2 1 ASN A 87 ? ? -164.05 59.98  
3 1 HIS B 20 ? ? -38.23  116.51 
4 1 ASN B 87 ? ? -169.27 61.83  
5 1 ASN C 87 ? ? -148.65 49.14  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            147.94 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.096 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       308 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.14 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ILE 28 ? B ILE 29 
4  1 Y 1 B ALA 29 ? B ALA 30 
5  1 Y 1 B ASP 30 ? B ASP 31 
6  1 Y 1 B GLY 31 ? B GLY 32 
7  1 Y 1 B ALA 32 ? B ALA 33 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
15 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H9V N1   N N N 1   
A1H9V N3   N Y N 2   
A1H9V C4   C Y N 3   
A1H9V C5   C Y N 4   
A1H9V C1   C N N 5   
A1H9V C2   C N N 6   
A1H9V C3   C Y N 7   
A1H9V N2   N Y N 8   
A1H9V O1   O N N 9   
A1H9V O2   O N N 10  
A1H9V S1   S N N 11  
A1H9V H8   H N N 12  
A1H9V H7   H N N 13  
A1H9V H9   H N N 14  
A1H9V H1   H N N 15  
A1H9V H3   H N N 16  
A1H9V H2   H N N 17  
A1H9V H5   H N N 18  
A1H9V H4   H N N 19  
A1H9V H6   H N N 20  
ALA   N    N N N 21  
ALA   CA   C N S 22  
ALA   C    C N N 23  
ALA   O    O N N 24  
ALA   CB   C N N 25  
ALA   OXT  O N N 26  
ALA   H    H N N 27  
ALA   H2   H N N 28  
ALA   HA   H N N 29  
ALA   HB1  H N N 30  
ALA   HB2  H N N 31  
ALA   HB3  H N N 32  
ALA   HXT  H N N 33  
ARG   N    N N N 34  
ARG   CA   C N S 35  
ARG   C    C N N 36  
ARG   O    O N N 37  
ARG   CB   C N N 38  
ARG   CG   C N N 39  
ARG   CD   C N N 40  
ARG   NE   N N N 41  
ARG   CZ   C N N 42  
ARG   NH1  N N N 43  
ARG   NH2  N N N 44  
ARG   OXT  O N N 45  
ARG   H    H N N 46  
ARG   H2   H N N 47  
ARG   HA   H N N 48  
ARG   HB2  H N N 49  
ARG   HB3  H N N 50  
ARG   HG2  H N N 51  
ARG   HG3  H N N 52  
ARG   HD2  H N N 53  
ARG   HD3  H N N 54  
ARG   HE   H N N 55  
ARG   HH11 H N N 56  
ARG   HH12 H N N 57  
ARG   HH21 H N N 58  
ARG   HH22 H N N 59  
ARG   HXT  H N N 60  
ASN   N    N N N 61  
ASN   CA   C N S 62  
ASN   C    C N N 63  
ASN   O    O N N 64  
ASN   CB   C N N 65  
ASN   CG   C N N 66  
ASN   OD1  O N N 67  
ASN   ND2  N N N 68  
ASN   OXT  O N N 69  
ASN   H    H N N 70  
ASN   H2   H N N 71  
ASN   HA   H N N 72  
ASN   HB2  H N N 73  
ASN   HB3  H N N 74  
ASN   HD21 H N N 75  
ASN   HD22 H N N 76  
ASN   HXT  H N N 77  
ASP   N    N N N 78  
ASP   CA   C N S 79  
ASP   C    C N N 80  
ASP   O    O N N 81  
ASP   CB   C N N 82  
ASP   CG   C N N 83  
ASP   OD1  O N N 84  
ASP   OD2  O N N 85  
ASP   OXT  O N N 86  
ASP   H    H N N 87  
ASP   H2   H N N 88  
ASP   HA   H N N 89  
ASP   HB2  H N N 90  
ASP   HB3  H N N 91  
ASP   HD2  H N N 92  
ASP   HXT  H N N 93  
CYS   N    N N N 94  
CYS   CA   C N R 95  
CYS   C    C N N 96  
CYS   O    O N N 97  
CYS   CB   C N N 98  
CYS   SG   S N N 99  
CYS   OXT  O N N 100 
CYS   H    H N N 101 
CYS   H2   H N N 102 
CYS   HA   H N N 103 
CYS   HB2  H N N 104 
CYS   HB3  H N N 105 
CYS   HG   H N N 106 
CYS   HXT  H N N 107 
EDO   C1   C N N 108 
EDO   O1   O N N 109 
EDO   C2   C N N 110 
EDO   O2   O N N 111 
EDO   H11  H N N 112 
EDO   H12  H N N 113 
EDO   HO1  H N N 114 
EDO   H21  H N N 115 
EDO   H22  H N N 116 
EDO   HO2  H N N 117 
GLN   N    N N N 118 
GLN   CA   C N S 119 
GLN   C    C N N 120 
GLN   O    O N N 121 
GLN   CB   C N N 122 
GLN   CG   C N N 123 
GLN   CD   C N N 124 
GLN   OE1  O N N 125 
GLN   NE2  N N N 126 
GLN   OXT  O N N 127 
GLN   H    H N N 128 
GLN   H2   H N N 129 
GLN   HA   H N N 130 
GLN   HB2  H N N 131 
GLN   HB3  H N N 132 
GLN   HG2  H N N 133 
GLN   HG3  H N N 134 
GLN   HE21 H N N 135 
GLN   HE22 H N N 136 
GLN   HXT  H N N 137 
GLU   N    N N N 138 
GLU   CA   C N S 139 
GLU   C    C N N 140 
GLU   O    O N N 141 
GLU   CB   C N N 142 
GLU   CG   C N N 143 
GLU   CD   C N N 144 
GLU   OE1  O N N 145 
GLU   OE2  O N N 146 
GLU   OXT  O N N 147 
GLU   H    H N N 148 
GLU   H2   H N N 149 
GLU   HA   H N N 150 
GLU   HB2  H N N 151 
GLU   HB3  H N N 152 
GLU   HG2  H N N 153 
GLU   HG3  H N N 154 
GLU   HE2  H N N 155 
GLU   HXT  H N N 156 
GLY   N    N N N 157 
GLY   CA   C N N 158 
GLY   C    C N N 159 
GLY   O    O N N 160 
GLY   OXT  O N N 161 
GLY   H    H N N 162 
GLY   H2   H N N 163 
GLY   HA2  H N N 164 
GLY   HA3  H N N 165 
GLY   HXT  H N N 166 
HIS   N    N N N 167 
HIS   CA   C N S 168 
HIS   C    C N N 169 
HIS   O    O N N 170 
HIS   CB   C N N 171 
HIS   CG   C Y N 172 
HIS   ND1  N Y N 173 
HIS   CD2  C Y N 174 
HIS   CE1  C Y N 175 
HIS   NE2  N Y N 176 
HIS   OXT  O N N 177 
HIS   H    H N N 178 
HIS   H2   H N N 179 
HIS   HA   H N N 180 
HIS   HB2  H N N 181 
HIS   HB3  H N N 182 
HIS   HD1  H N N 183 
HIS   HD2  H N N 184 
HIS   HE1  H N N 185 
HIS   HE2  H N N 186 
HIS   HXT  H N N 187 
HOH   O    O N N 188 
HOH   H1   H N N 189 
HOH   H2   H N N 190 
ILE   N    N N N 191 
ILE   CA   C N S 192 
ILE   C    C N N 193 
ILE   O    O N N 194 
ILE   CB   C N S 195 
ILE   CG1  C N N 196 
ILE   CG2  C N N 197 
ILE   CD1  C N N 198 
ILE   OXT  O N N 199 
ILE   H    H N N 200 
ILE   H2   H N N 201 
ILE   HA   H N N 202 
ILE   HB   H N N 203 
ILE   HG12 H N N 204 
ILE   HG13 H N N 205 
ILE   HG21 H N N 206 
ILE   HG22 H N N 207 
ILE   HG23 H N N 208 
ILE   HD11 H N N 209 
ILE   HD12 H N N 210 
ILE   HD13 H N N 211 
ILE   HXT  H N N 212 
LEU   N    N N N 213 
LEU   CA   C N S 214 
LEU   C    C N N 215 
LEU   O    O N N 216 
LEU   CB   C N N 217 
LEU   CG   C N N 218 
LEU   CD1  C N N 219 
LEU   CD2  C N N 220 
LEU   OXT  O N N 221 
LEU   H    H N N 222 
LEU   H2   H N N 223 
LEU   HA   H N N 224 
LEU   HB2  H N N 225 
LEU   HB3  H N N 226 
LEU   HG   H N N 227 
LEU   HD11 H N N 228 
LEU   HD12 H N N 229 
LEU   HD13 H N N 230 
LEU   HD21 H N N 231 
LEU   HD22 H N N 232 
LEU   HD23 H N N 233 
LEU   HXT  H N N 234 
LYS   N    N N N 235 
LYS   CA   C N S 236 
LYS   C    C N N 237 
LYS   O    O N N 238 
LYS   CB   C N N 239 
LYS   CG   C N N 240 
LYS   CD   C N N 241 
LYS   CE   C N N 242 
LYS   NZ   N N N 243 
LYS   OXT  O N N 244 
LYS   H    H N N 245 
LYS   H2   H N N 246 
LYS   HA   H N N 247 
LYS   HB2  H N N 248 
LYS   HB3  H N N 249 
LYS   HG2  H N N 250 
LYS   HG3  H N N 251 
LYS   HD2  H N N 252 
LYS   HD3  H N N 253 
LYS   HE2  H N N 254 
LYS   HE3  H N N 255 
LYS   HZ1  H N N 256 
LYS   HZ2  H N N 257 
LYS   HZ3  H N N 258 
LYS   HXT  H N N 259 
MET   N    N N N 260 
MET   CA   C N S 261 
MET   C    C N N 262 
MET   O    O N N 263 
MET   CB   C N N 264 
MET   CG   C N N 265 
MET   SD   S N N 266 
MET   CE   C N N 267 
MET   OXT  O N N 268 
MET   H    H N N 269 
MET   H2   H N N 270 
MET   HA   H N N 271 
MET   HB2  H N N 272 
MET   HB3  H N N 273 
MET   HG2  H N N 274 
MET   HG3  H N N 275 
MET   HE1  H N N 276 
MET   HE2  H N N 277 
MET   HE3  H N N 278 
MET   HXT  H N N 279 
PHE   N    N N N 280 
PHE   CA   C N S 281 
PHE   C    C N N 282 
PHE   O    O N N 283 
PHE   CB   C N N 284 
PHE   CG   C Y N 285 
PHE   CD1  C Y N 286 
PHE   CD2  C Y N 287 
PHE   CE1  C Y N 288 
PHE   CE2  C Y N 289 
PHE   CZ   C Y N 290 
PHE   OXT  O N N 291 
PHE   H    H N N 292 
PHE   H2   H N N 293 
PHE   HA   H N N 294 
PHE   HB2  H N N 295 
PHE   HB3  H N N 296 
PHE   HD1  H N N 297 
PHE   HD2  H N N 298 
PHE   HE1  H N N 299 
PHE   HE2  H N N 300 
PHE   HZ   H N N 301 
PHE   HXT  H N N 302 
PRO   N    N N N 303 
PRO   CA   C N S 304 
PRO   C    C N N 305 
PRO   O    O N N 306 
PRO   CB   C N N 307 
PRO   CG   C N N 308 
PRO   CD   C N N 309 
PRO   OXT  O N N 310 
PRO   H    H N N 311 
PRO   HA   H N N 312 
PRO   HB2  H N N 313 
PRO   HB3  H N N 314 
PRO   HG2  H N N 315 
PRO   HG3  H N N 316 
PRO   HD2  H N N 317 
PRO   HD3  H N N 318 
PRO   HXT  H N N 319 
SER   N    N N N 320 
SER   CA   C N S 321 
SER   C    C N N 322 
SER   O    O N N 323 
SER   CB   C N N 324 
SER   OG   O N N 325 
SER   OXT  O N N 326 
SER   H    H N N 327 
SER   H2   H N N 328 
SER   HA   H N N 329 
SER   HB2  H N N 330 
SER   HB3  H N N 331 
SER   HG   H N N 332 
SER   HXT  H N N 333 
SO4   S    S N N 334 
SO4   O1   O N N 335 
SO4   O2   O N N 336 
SO4   O3   O N N 337 
SO4   O4   O N N 338 
THR   N    N N N 339 
THR   CA   C N S 340 
THR   C    C N N 341 
THR   O    O N N 342 
THR   CB   C N R 343 
THR   OG1  O N N 344 
THR   CG2  C N N 345 
THR   OXT  O N N 346 
THR   H    H N N 347 
THR   H2   H N N 348 
THR   HA   H N N 349 
THR   HB   H N N 350 
THR   HG1  H N N 351 
THR   HG21 H N N 352 
THR   HG22 H N N 353 
THR   HG23 H N N 354 
THR   HXT  H N N 355 
TRP   N    N N N 356 
TRP   CA   C N S 357 
TRP   C    C N N 358 
TRP   O    O N N 359 
TRP   CB   C N N 360 
TRP   CG   C Y N 361 
TRP   CD1  C Y N 362 
TRP   CD2  C Y N 363 
TRP   NE1  N Y N 364 
TRP   CE2  C Y N 365 
TRP   CE3  C Y N 366 
TRP   CZ2  C Y N 367 
TRP   CZ3  C Y N 368 
TRP   CH2  C Y N 369 
TRP   OXT  O N N 370 
TRP   H    H N N 371 
TRP   H2   H N N 372 
TRP   HA   H N N 373 
TRP   HB2  H N N 374 
TRP   HB3  H N N 375 
TRP   HD1  H N N 376 
TRP   HE1  H N N 377 
TRP   HE3  H N N 378 
TRP   HZ2  H N N 379 
TRP   HZ3  H N N 380 
TRP   HH2  H N N 381 
TRP   HXT  H N N 382 
TYR   N    N N N 383 
TYR   CA   C N S 384 
TYR   C    C N N 385 
TYR   O    O N N 386 
TYR   CB   C N N 387 
TYR   CG   C Y N 388 
TYR   CD1  C Y N 389 
TYR   CD2  C Y N 390 
TYR   CE1  C Y N 391 
TYR   CE2  C Y N 392 
TYR   CZ   C Y N 393 
TYR   OH   O N N 394 
TYR   OXT  O N N 395 
TYR   H    H N N 396 
TYR   H2   H N N 397 
TYR   HA   H N N 398 
TYR   HB2  H N N 399 
TYR   HB3  H N N 400 
TYR   HD1  H N N 401 
TYR   HD2  H N N 402 
TYR   HE1  H N N 403 
TYR   HE2  H N N 404 
TYR   HH   H N N 405 
TYR   HXT  H N N 406 
VAL   N    N N N 407 
VAL   CA   C N S 408 
VAL   C    C N N 409 
VAL   O    O N N 410 
VAL   CB   C N N 411 
VAL   CG1  C N N 412 
VAL   CG2  C N N 413 
VAL   OXT  O N N 414 
VAL   H    H N N 415 
VAL   H2   H N N 416 
VAL   HA   H N N 417 
VAL   HB   H N N 418 
VAL   HG11 H N N 419 
VAL   HG12 H N N 420 
VAL   HG13 H N N 421 
VAL   HG21 H N N 422 
VAL   HG22 H N N 423 
VAL   HG23 H N N 424 
VAL   HXT  H N N 425 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1H9V C1  N1   sing N N 1   
A1H9V N1  C2   sing N N 2   
A1H9V N1  S1   sing N N 3   
A1H9V S1  O1   doub N N 4   
A1H9V S1  O2   doub N N 5   
A1H9V S1  C3   sing N N 6   
A1H9V C3  C4   sing Y N 7   
A1H9V C4  N2   doub Y N 8   
A1H9V N2  N3   sing Y N 9   
A1H9V N3  C5   sing Y N 10  
A1H9V C3  C5   doub Y N 11  
A1H9V N3  H8   sing N N 12  
A1H9V C4  H7   sing N N 13  
A1H9V C5  H9   sing N N 14  
A1H9V C1  H1   sing N N 15  
A1H9V C1  H3   sing N N 16  
A1H9V C1  H2   sing N N 17  
A1H9V C2  H5   sing N N 18  
A1H9V C2  H4   sing N N 19  
A1H9V C2  H6   sing N N 20  
ALA   N   CA   sing N N 21  
ALA   N   H    sing N N 22  
ALA   N   H2   sing N N 23  
ALA   CA  C    sing N N 24  
ALA   CA  CB   sing N N 25  
ALA   CA  HA   sing N N 26  
ALA   C   O    doub N N 27  
ALA   C   OXT  sing N N 28  
ALA   CB  HB1  sing N N 29  
ALA   CB  HB2  sing N N 30  
ALA   CB  HB3  sing N N 31  
ALA   OXT HXT  sing N N 32  
ARG   N   CA   sing N N 33  
ARG   N   H    sing N N 34  
ARG   N   H2   sing N N 35  
ARG   CA  C    sing N N 36  
ARG   CA  CB   sing N N 37  
ARG   CA  HA   sing N N 38  
ARG   C   O    doub N N 39  
ARG   C   OXT  sing N N 40  
ARG   CB  CG   sing N N 41  
ARG   CB  HB2  sing N N 42  
ARG   CB  HB3  sing N N 43  
ARG   CG  CD   sing N N 44  
ARG   CG  HG2  sing N N 45  
ARG   CG  HG3  sing N N 46  
ARG   CD  NE   sing N N 47  
ARG   CD  HD2  sing N N 48  
ARG   CD  HD3  sing N N 49  
ARG   NE  CZ   sing N N 50  
ARG   NE  HE   sing N N 51  
ARG   CZ  NH1  sing N N 52  
ARG   CZ  NH2  doub N N 53  
ARG   NH1 HH11 sing N N 54  
ARG   NH1 HH12 sing N N 55  
ARG   NH2 HH21 sing N N 56  
ARG   NH2 HH22 sing N N 57  
ARG   OXT HXT  sing N N 58  
ASN   N   CA   sing N N 59  
ASN   N   H    sing N N 60  
ASN   N   H2   sing N N 61  
ASN   CA  C    sing N N 62  
ASN   CA  CB   sing N N 63  
ASN   CA  HA   sing N N 64  
ASN   C   O    doub N N 65  
ASN   C   OXT  sing N N 66  
ASN   CB  CG   sing N N 67  
ASN   CB  HB2  sing N N 68  
ASN   CB  HB3  sing N N 69  
ASN   CG  OD1  doub N N 70  
ASN   CG  ND2  sing N N 71  
ASN   ND2 HD21 sing N N 72  
ASN   ND2 HD22 sing N N 73  
ASN   OXT HXT  sing N N 74  
ASP   N   CA   sing N N 75  
ASP   N   H    sing N N 76  
ASP   N   H2   sing N N 77  
ASP   CA  C    sing N N 78  
ASP   CA  CB   sing N N 79  
ASP   CA  HA   sing N N 80  
ASP   C   O    doub N N 81  
ASP   C   OXT  sing N N 82  
ASP   CB  CG   sing N N 83  
ASP   CB  HB2  sing N N 84  
ASP   CB  HB3  sing N N 85  
ASP   CG  OD1  doub N N 86  
ASP   CG  OD2  sing N N 87  
ASP   OD2 HD2  sing N N 88  
ASP   OXT HXT  sing N N 89  
CYS   N   CA   sing N N 90  
CYS   N   H    sing N N 91  
CYS   N   H2   sing N N 92  
CYS   CA  C    sing N N 93  
CYS   CA  CB   sing N N 94  
CYS   CA  HA   sing N N 95  
CYS   C   O    doub N N 96  
CYS   C   OXT  sing N N 97  
CYS   CB  SG   sing N N 98  
CYS   CB  HB2  sing N N 99  
CYS   CB  HB3  sing N N 100 
CYS   SG  HG   sing N N 101 
CYS   OXT HXT  sing N N 102 
EDO   C1  O1   sing N N 103 
EDO   C1  C2   sing N N 104 
EDO   C1  H11  sing N N 105 
EDO   C1  H12  sing N N 106 
EDO   O1  HO1  sing N N 107 
EDO   C2  O2   sing N N 108 
EDO   C2  H21  sing N N 109 
EDO   C2  H22  sing N N 110 
EDO   O2  HO2  sing N N 111 
GLN   N   CA   sing N N 112 
GLN   N   H    sing N N 113 
GLN   N   H2   sing N N 114 
GLN   CA  C    sing N N 115 
GLN   CA  CB   sing N N 116 
GLN   CA  HA   sing N N 117 
GLN   C   O    doub N N 118 
GLN   C   OXT  sing N N 119 
GLN   CB  CG   sing N N 120 
GLN   CB  HB2  sing N N 121 
GLN   CB  HB3  sing N N 122 
GLN   CG  CD   sing N N 123 
GLN   CG  HG2  sing N N 124 
GLN   CG  HG3  sing N N 125 
GLN   CD  OE1  doub N N 126 
GLN   CD  NE2  sing N N 127 
GLN   NE2 HE21 sing N N 128 
GLN   NE2 HE22 sing N N 129 
GLN   OXT HXT  sing N N 130 
GLU   N   CA   sing N N 131 
GLU   N   H    sing N N 132 
GLU   N   H2   sing N N 133 
GLU   CA  C    sing N N 134 
GLU   CA  CB   sing N N 135 
GLU   CA  HA   sing N N 136 
GLU   C   O    doub N N 137 
GLU   C   OXT  sing N N 138 
GLU   CB  CG   sing N N 139 
GLU   CB  HB2  sing N N 140 
GLU   CB  HB3  sing N N 141 
GLU   CG  CD   sing N N 142 
GLU   CG  HG2  sing N N 143 
GLU   CG  HG3  sing N N 144 
GLU   CD  OE1  doub N N 145 
GLU   CD  OE2  sing N N 146 
GLU   OE2 HE2  sing N N 147 
GLU   OXT HXT  sing N N 148 
GLY   N   CA   sing N N 149 
GLY   N   H    sing N N 150 
GLY   N   H2   sing N N 151 
GLY   CA  C    sing N N 152 
GLY   CA  HA2  sing N N 153 
GLY   CA  HA3  sing N N 154 
GLY   C   O    doub N N 155 
GLY   C   OXT  sing N N 156 
GLY   OXT HXT  sing N N 157 
HIS   N   CA   sing N N 158 
HIS   N   H    sing N N 159 
HIS   N   H2   sing N N 160 
HIS   CA  C    sing N N 161 
HIS   CA  CB   sing N N 162 
HIS   CA  HA   sing N N 163 
HIS   C   O    doub N N 164 
HIS   C   OXT  sing N N 165 
HIS   CB  CG   sing N N 166 
HIS   CB  HB2  sing N N 167 
HIS   CB  HB3  sing N N 168 
HIS   CG  ND1  sing Y N 169 
HIS   CG  CD2  doub Y N 170 
HIS   ND1 CE1  doub Y N 171 
HIS   ND1 HD1  sing N N 172 
HIS   CD2 NE2  sing Y N 173 
HIS   CD2 HD2  sing N N 174 
HIS   CE1 NE2  sing Y N 175 
HIS   CE1 HE1  sing N N 176 
HIS   NE2 HE2  sing N N 177 
HIS   OXT HXT  sing N N 178 
HOH   O   H1   sing N N 179 
HOH   O   H2   sing N N 180 
ILE   N   CA   sing N N 181 
ILE   N   H    sing N N 182 
ILE   N   H2   sing N N 183 
ILE   CA  C    sing N N 184 
ILE   CA  CB   sing N N 185 
ILE   CA  HA   sing N N 186 
ILE   C   O    doub N N 187 
ILE   C   OXT  sing N N 188 
ILE   CB  CG1  sing N N 189 
ILE   CB  CG2  sing N N 190 
ILE   CB  HB   sing N N 191 
ILE   CG1 CD1  sing N N 192 
ILE   CG1 HG12 sing N N 193 
ILE   CG1 HG13 sing N N 194 
ILE   CG2 HG21 sing N N 195 
ILE   CG2 HG22 sing N N 196 
ILE   CG2 HG23 sing N N 197 
ILE   CD1 HD11 sing N N 198 
ILE   CD1 HD12 sing N N 199 
ILE   CD1 HD13 sing N N 200 
ILE   OXT HXT  sing N N 201 
LEU   N   CA   sing N N 202 
LEU   N   H    sing N N 203 
LEU   N   H2   sing N N 204 
LEU   CA  C    sing N N 205 
LEU   CA  CB   sing N N 206 
LEU   CA  HA   sing N N 207 
LEU   C   O    doub N N 208 
LEU   C   OXT  sing N N 209 
LEU   CB  CG   sing N N 210 
LEU   CB  HB2  sing N N 211 
LEU   CB  HB3  sing N N 212 
LEU   CG  CD1  sing N N 213 
LEU   CG  CD2  sing N N 214 
LEU   CG  HG   sing N N 215 
LEU   CD1 HD11 sing N N 216 
LEU   CD1 HD12 sing N N 217 
LEU   CD1 HD13 sing N N 218 
LEU   CD2 HD21 sing N N 219 
LEU   CD2 HD22 sing N N 220 
LEU   CD2 HD23 sing N N 221 
LEU   OXT HXT  sing N N 222 
LYS   N   CA   sing N N 223 
LYS   N   H    sing N N 224 
LYS   N   H2   sing N N 225 
LYS   CA  C    sing N N 226 
LYS   CA  CB   sing N N 227 
LYS   CA  HA   sing N N 228 
LYS   C   O    doub N N 229 
LYS   C   OXT  sing N N 230 
LYS   CB  CG   sing N N 231 
LYS   CB  HB2  sing N N 232 
LYS   CB  HB3  sing N N 233 
LYS   CG  CD   sing N N 234 
LYS   CG  HG2  sing N N 235 
LYS   CG  HG3  sing N N 236 
LYS   CD  CE   sing N N 237 
LYS   CD  HD2  sing N N 238 
LYS   CD  HD3  sing N N 239 
LYS   CE  NZ   sing N N 240 
LYS   CE  HE2  sing N N 241 
LYS   CE  HE3  sing N N 242 
LYS   NZ  HZ1  sing N N 243 
LYS   NZ  HZ2  sing N N 244 
LYS   NZ  HZ3  sing N N 245 
LYS   OXT HXT  sing N N 246 
MET   N   CA   sing N N 247 
MET   N   H    sing N N 248 
MET   N   H2   sing N N 249 
MET   CA  C    sing N N 250 
MET   CA  CB   sing N N 251 
MET   CA  HA   sing N N 252 
MET   C   O    doub N N 253 
MET   C   OXT  sing N N 254 
MET   CB  CG   sing N N 255 
MET   CB  HB2  sing N N 256 
MET   CB  HB3  sing N N 257 
MET   CG  SD   sing N N 258 
MET   CG  HG2  sing N N 259 
MET   CG  HG3  sing N N 260 
MET   SD  CE   sing N N 261 
MET   CE  HE1  sing N N 262 
MET   CE  HE2  sing N N 263 
MET   CE  HE3  sing N N 264 
MET   OXT HXT  sing N N 265 
PHE   N   CA   sing N N 266 
PHE   N   H    sing N N 267 
PHE   N   H2   sing N N 268 
PHE   CA  C    sing N N 269 
PHE   CA  CB   sing N N 270 
PHE   CA  HA   sing N N 271 
PHE   C   O    doub N N 272 
PHE   C   OXT  sing N N 273 
PHE   CB  CG   sing N N 274 
PHE   CB  HB2  sing N N 275 
PHE   CB  HB3  sing N N 276 
PHE   CG  CD1  doub Y N 277 
PHE   CG  CD2  sing Y N 278 
PHE   CD1 CE1  sing Y N 279 
PHE   CD1 HD1  sing N N 280 
PHE   CD2 CE2  doub Y N 281 
PHE   CD2 HD2  sing N N 282 
PHE   CE1 CZ   doub Y N 283 
PHE   CE1 HE1  sing N N 284 
PHE   CE2 CZ   sing Y N 285 
PHE   CE2 HE2  sing N N 286 
PHE   CZ  HZ   sing N N 287 
PHE   OXT HXT  sing N N 288 
PRO   N   CA   sing N N 289 
PRO   N   CD   sing N N 290 
PRO   N   H    sing N N 291 
PRO   CA  C    sing N N 292 
PRO   CA  CB   sing N N 293 
PRO   CA  HA   sing N N 294 
PRO   C   O    doub N N 295 
PRO   C   OXT  sing N N 296 
PRO   CB  CG   sing N N 297 
PRO   CB  HB2  sing N N 298 
PRO   CB  HB3  sing N N 299 
PRO   CG  CD   sing N N 300 
PRO   CG  HG2  sing N N 301 
PRO   CG  HG3  sing N N 302 
PRO   CD  HD2  sing N N 303 
PRO   CD  HD3  sing N N 304 
PRO   OXT HXT  sing N N 305 
SER   N   CA   sing N N 306 
SER   N   H    sing N N 307 
SER   N   H2   sing N N 308 
SER   CA  C    sing N N 309 
SER   CA  CB   sing N N 310 
SER   CA  HA   sing N N 311 
SER   C   O    doub N N 312 
SER   C   OXT  sing N N 313 
SER   CB  OG   sing N N 314 
SER   CB  HB2  sing N N 315 
SER   CB  HB3  sing N N 316 
SER   OG  HG   sing N N 317 
SER   OXT HXT  sing N N 318 
SO4   S   O1   doub N N 319 
SO4   S   O2   doub N N 320 
SO4   S   O3   sing N N 321 
SO4   S   O4   sing N N 322 
THR   N   CA   sing N N 323 
THR   N   H    sing N N 324 
THR   N   H2   sing N N 325 
THR   CA  C    sing N N 326 
THR   CA  CB   sing N N 327 
THR   CA  HA   sing N N 328 
THR   C   O    doub N N 329 
THR   C   OXT  sing N N 330 
THR   CB  OG1  sing N N 331 
THR   CB  CG2  sing N N 332 
THR   CB  HB   sing N N 333 
THR   OG1 HG1  sing N N 334 
THR   CG2 HG21 sing N N 335 
THR   CG2 HG22 sing N N 336 
THR   CG2 HG23 sing N N 337 
THR   OXT HXT  sing N N 338 
TRP   N   CA   sing N N 339 
TRP   N   H    sing N N 340 
TRP   N   H2   sing N N 341 
TRP   CA  C    sing N N 342 
TRP   CA  CB   sing N N 343 
TRP   CA  HA   sing N N 344 
TRP   C   O    doub N N 345 
TRP   C   OXT  sing N N 346 
TRP   CB  CG   sing N N 347 
TRP   CB  HB2  sing N N 348 
TRP   CB  HB3  sing N N 349 
TRP   CG  CD1  doub Y N 350 
TRP   CG  CD2  sing Y N 351 
TRP   CD1 NE1  sing Y N 352 
TRP   CD1 HD1  sing N N 353 
TRP   CD2 CE2  doub Y N 354 
TRP   CD2 CE3  sing Y N 355 
TRP   NE1 CE2  sing Y N 356 
TRP   NE1 HE1  sing N N 357 
TRP   CE2 CZ2  sing Y N 358 
TRP   CE3 CZ3  doub Y N 359 
TRP   CE3 HE3  sing N N 360 
TRP   CZ2 CH2  doub Y N 361 
TRP   CZ2 HZ2  sing N N 362 
TRP   CZ3 CH2  sing Y N 363 
TRP   CZ3 HZ3  sing N N 364 
TRP   CH2 HH2  sing N N 365 
TRP   OXT HXT  sing N N 366 
TYR   N   CA   sing N N 367 
TYR   N   H    sing N N 368 
TYR   N   H2   sing N N 369 
TYR   CA  C    sing N N 370 
TYR   CA  CB   sing N N 371 
TYR   CA  HA   sing N N 372 
TYR   C   O    doub N N 373 
TYR   C   OXT  sing N N 374 
TYR   CB  CG   sing N N 375 
TYR   CB  HB2  sing N N 376 
TYR   CB  HB3  sing N N 377 
TYR   CG  CD1  doub Y N 378 
TYR   CG  CD2  sing Y N 379 
TYR   CD1 CE1  sing Y N 380 
TYR   CD1 HD1  sing N N 381 
TYR   CD2 CE2  doub Y N 382 
TYR   CD2 HD2  sing N N 383 
TYR   CE1 CZ   doub Y N 384 
TYR   CE1 HE1  sing N N 385 
TYR   CE2 CZ   sing Y N 386 
TYR   CE2 HE2  sing N N 387 
TYR   CZ  OH   sing N N 388 
TYR   OH  HH   sing N N 389 
TYR   OXT HXT  sing N N 390 
VAL   N   CA   sing N N 391 
VAL   N   H    sing N N 392 
VAL   N   H2   sing N N 393 
VAL   CA  C    sing N N 394 
VAL   CA  CB   sing N N 395 
VAL   CA  HA   sing N N 396 
VAL   C   O    doub N N 397 
VAL   C   OXT  sing N N 398 
VAL   CB  CG1  sing N N 399 
VAL   CB  CG2  sing N N 400 
VAL   CB  HB   sing N N 401 
VAL   CG1 HG11 sing N N 402 
VAL   CG1 HG12 sing N N 403 
VAL   CG1 HG13 sing N N 404 
VAL   CG2 HG21 sing N N 405 
VAL   CG2 HG22 sing N N 406 
VAL   CG2 HG23 sing N N 407 
VAL   OXT HXT  sing N N 408 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HHI 
_atom_sites.fract_transf_matrix[1][1]   0.024145 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023917 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006341 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET   A 1 2  ? 0.307   4.486   2.456   1.00 69.13  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.723  3.704   1.720   1.00 73.65  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? -0.063  2.612   0.869   1.00 67.46  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.120   2.700   0.524   1.00 58.68  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.646  4.604   0.884   1.00 72.98  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.665  5.437   1.676   1.00 79.02  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.795  4.698   2.880   1.00 88.52  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -2.812  4.868   4.379   1.00 79.92  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.798  1.514   0.557   1.00 56.57  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.266  0.410   -0.245  1.00 58.64  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? -0.107  0.731   -1.730  1.00 52.76  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.881  1.487   -2.325  1.00 41.84  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.288  -0.739  -0.005  1.00 63.74  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -2.106  -0.276  1.186   1.00 62.46  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -2.164  1.234   1.024   1.00 59.52  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 0.941   0.165   -2.318  1.00 45.93  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.100   0.331   -3.746  1.00 44.92  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.477   -0.926  -4.334  1.00 47.14  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? -0.107  -1.691  -3.569  1.00 39.36  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.576   0.576   -4.082  1.00 50.47  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.244   1.698   -3.345  1.00 61.55  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 4.182   2.513   -3.951  1.00 65.49  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 3.135   2.147   -2.079  1.00 66.45  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.613   3.421   -3.085  1.00 67.24  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 3.989   3.219   -1.939  1.00 70.61  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.604   -1.121  -5.660  1.00 43.07  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.337   -2.398  -6.306  1.00 37.97  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.429   -3.409  -5.921  1.00 39.91  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.490   -3.018  -5.431  1.00 35.19  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.273   -2.177  -7.807  1.00 38.61  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.162   -4.712  -6.117  1.00 34.00  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.161   -5.753  -5.868  1.00 36.54  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.312   -5.635  -6.877  1.00 41.72  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.081   -5.483  -8.087  1.00 42.82  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.526   -7.157  -5.891  1.00 28.42  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 0.806   -7.538  -4.607  1.00 27.92  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.469   -7.512  -3.378  1.00 28.77  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.541  -7.902  -4.616  1.00 26.60  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 0.804   -7.841  -2.198  1.00 28.13  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -1.191  -8.261  -3.429  1.00 27.85  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.526  -8.206  -2.218  1.00 28.46  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.550   -5.748  -6.372  1.00 35.77  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 5.734   -5.718  -7.217  1.00 38.18  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.628   -6.917  -6.910  1.00 36.37  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.577   -7.468  -5.809  1.00 41.26  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.486   -4.405  -7.017  1.00 38.06  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.038   -4.231  -5.609  1.00 47.36  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.786   -2.909  -5.469  1.00 46.80  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.609   -2.828  -4.222  1.00 44.84  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.814   -3.111  -3.035  1.00 46.29  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.457   -7.374  -7.875  1.00 31.96  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.298   -8.557  -7.669  1.00 33.71  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.146   -8.261  -6.447  1.00 32.70  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 9.598   -7.139  -6.295  1.00 45.08  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.131   -8.609  -8.948  1.00 31.24  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.241   -7.945  -9.974  1.00 36.05  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.597   -6.806  -9.223  1.00 30.95  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.292   -9.242  -5.558  1.00 34.29  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.046  -9.089  -4.326  1.00 30.75  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.127   -9.011  -3.108  1.00 35.33  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.589   -9.143  -1.967  1.00 37.47  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 7.830   -8.799  -3.353  1.00 31.26  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 6.882   -8.687  -2.255  1.00 34.44  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 6.653   -10.060 -1.636  1.00 31.63  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.541   -11.041 -2.364  1.00 34.37  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.584   -7.998  -2.671  1.00 33.21  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 5.655   -6.498  -2.911  1.00 36.14  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.663   -5.890  -2.538  1.00 36.54  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 4.667   -5.939  -3.457  1.00 42.48  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.594   -10.109 -0.294  1.00 31.33  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.378   -11.340 0.447   1.00 32.93  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 4.905   -11.459 0.852   1.00 38.13  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.259   -10.479 1.239   1.00 41.56  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.291   -11.374 1.666   1.00 32.38  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 8.792   -11.135 1.459   1.00 31.36  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 9.515   -11.314 2.791   1.00 28.64  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.456   -12.022 0.436   1.00 31.70  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.340   -12.661 0.716   1.00 35.93  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 2.890   -12.802 0.851   1.00 35.07  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 2.635   -14.148 1.492   1.00 28.70  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.537   -14.953 1.548   1.00 29.52  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.179   -12.822 -0.517  1.00 35.73  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.497   -11.556 -1.301  1.00 35.85  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.560   -14.087 -1.295  1.00 22.48  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.430   -14.338 2.005   1.00 27.92  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 0.812   -15.653 2.069   1.00 28.18  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? -0.075  -15.727 0.836   1.00 27.45  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.804  -14.786 0.549   1.00 30.22  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.029   -15.898 3.362   1.00 27.71  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 0.974   -16.119 4.543   1.00 32.10  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.400   -15.059 5.329   1.00 33.80  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.542   -17.372 4.778   1.00 34.93  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.293   -15.257 6.374   1.00 36.45  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.408   -17.576 5.846   1.00 35.58  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 2.788   -16.522 6.632   1.00 37.41  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.042   -16.811 0.076   1.00 30.33  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.777  -16.969 -1.114  1.00 35.32  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.763  -18.124 -0.922  1.00 38.52  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -1.385  -19.218 -0.484  1.00 39.01  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.086   -17.083 -2.365  1.00 29.00  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -3.043  -17.857 -1.236  1.00 41.16  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -4.087  -18.842 -1.007  1.00 44.49  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -4.466  -19.571 -2.299  1.00 46.05  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -5.022  -18.987 -3.227  1.00 43.13  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -5.296  -18.205 -0.315  1.00 41.11  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -6.327  -19.223 0.114   1.00 47.90  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.836  -20.220 1.159   1.00 55.46  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.898  -21.174 1.629   1.00 46.17  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -7.065  -22.219 0.621   1.00 43.93  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -4.202  -20.877 -2.300  1.00 48.04  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.674  -21.792 -3.323  1.00 52.82  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.846  -22.605 -2.776  1.00 52.23  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.893  -22.897 -1.581  1.00 43.99  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.577  -22.805 -3.660  1.00 56.81  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.291  -22.218 -4.226  1.00 64.15  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -2.345  -21.664 -5.946  1.00 57.15  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -3.375  -22.894 -6.758  1.00 63.56  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.754  -23.010 -3.673  1.00 52.42  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.872  -23.876 -3.311  1.00 58.83  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -7.329  -25.182 -2.753  1.00 52.51  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -6.509  -25.840 -3.386  1.00 58.38  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.797  -24.226 -4.486  1.00 66.64  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -10.190 -24.641 -4.017  1.00 75.28  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -11.353 -24.537 -5.001  1.00 72.03  ? 16  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 17 ? -12.663 -24.837 -4.316  1.00 69.31  ? 16  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 17 ? -13.810 -24.872 -5.225  1.00 66.67  ? 16  LYS   A NZ  1 
ATOM   127  N N   . GLY   A 1 18 ? -7.752  -25.517 -1.539  1.00 48.67  ? 17  GLY   A N   1 
ATOM   128  C CA  . GLY   A 1 18 ? -7.356  -26.789 -0.964  1.00 50.64  ? 17  GLY   A CA  1 
ATOM   129  C C   . GLY   A 1 18 ? -6.054  -26.716 -0.174  1.00 48.46  ? 17  GLY   A C   1 
ATOM   130  O O   . GLY   A 1 18 ? -5.715  -27.653 0.531   1.00 50.75  ? 17  GLY   A O   1 
ATOM   131  N N   . TYR   A 1 19 ? -5.300  -25.625 -0.293  1.00 48.96  ? 18  TYR   A N   1 
ATOM   132  C CA  . TYR   A 1 19 ? -4.093  -25.516 0.512   1.00 43.81  ? 18  TYR   A CA  1 
ATOM   133  C C   . TYR   A 1 19 ? -4.319  -24.411 1.524   1.00 42.47  ? 18  TYR   A C   1 
ATOM   134  O O   . TYR   A 1 19 ? -5.148  -23.537 1.280   1.00 38.98  ? 18  TYR   A O   1 
ATOM   135  C CB  . TYR   A 1 19 ? -2.843  -25.241 -0.321  1.00 45.65  ? 18  TYR   A CB  1 
ATOM   136  C CG  . TYR   A 1 19 ? -2.664  -26.228 -1.462  1.00 53.21  ? 18  TYR   A CG  1 
ATOM   137  C CD1 . TYR   A 1 19 ? -2.104  -27.492 -1.252  1.00 57.46  ? 18  TYR   A CD1 1 
ATOM   138  C CD2 . TYR   A 1 19 ? -3.075  -25.893 -2.752  1.00 59.05  ? 18  TYR   A CD2 1 
ATOM   139  C CE1 . TYR   A 1 19 ? -1.965  -28.388 -2.305  1.00 65.41  ? 18  TYR   A CE1 1 
ATOM   140  C CE2 . TYR   A 1 19 ? -2.929  -26.778 -3.812  1.00 63.88  ? 18  TYR   A CE2 1 
ATOM   141  C CZ  . TYR   A 1 19 ? -2.376  -28.032 -3.587  1.00 69.03  ? 18  TYR   A CZ  1 
ATOM   142  O OH  . TYR   A 1 19 ? -2.257  -28.887 -4.658  1.00 72.78  ? 18  TYR   A OH  1 
ATOM   143  N N   . PRO   A 1 20 ? -3.624  -24.407 2.684   1.00 40.24  ? 19  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 20 ? -3.738  -23.282 3.614   1.00 43.34  ? 19  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 20 ? -2.961  -22.098 3.030   1.00 39.80  ? 19  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 20 ? -2.155  -22.268 2.107   1.00 35.03  ? 19  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 20 ? -3.163  -23.814 4.941   1.00 40.87  ? 19  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 20 ? -2.177  -24.872 4.502   1.00 39.11  ? 19  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 20 ? -2.683  -25.427 3.155   1.00 41.23  ? 19  PRO   A CD  1 
ATOM   150  N N   . HIS   A 1 21 ? -3.253  -20.890 3.529   1.00 36.08  ? 20  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 21 ? -2.411  -19.743 3.217   1.00 39.96  ? 20  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 21 ? -0.940  -20.172 3.285   1.00 46.77  ? 20  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 21 ? -0.507  -20.756 4.285   1.00 49.39  ? 20  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 21 ? -2.828  -18.538 4.067   1.00 39.48  ? 20  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 21 ? -4.274  -18.184 3.890   1.00 42.01  ? 20  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 21 ? -5.302  -18.899 4.480   1.00 43.18  ? 20  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 21 ? -4.864  -17.221 3.175   1.00 40.62  ? 20  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 21 ? -6.464  -18.385 4.140   1.00 37.84  ? 20  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 21 ? -6.226  -17.356 3.355   1.00 45.39  ? 20  HIS   A NE2 1 
ATOM   160  N N   . TRP   A 1 22 ? -0.190  -19.899 2.197   1.00 44.33  ? 21  TRP   A N   1 
ATOM   161  C CA  . TRP   A 1 22 ? 1.148   -20.457 1.988   1.00 45.07  ? 21  TRP   A CA  1 
ATOM   162  C C   . TRP   A 1 22 ? 2.203   -19.349 1.811   1.00 40.42  ? 21  TRP   A C   1 
ATOM   163  O O   . TRP   A 1 22 ? 1.980   -18.384 1.067   1.00 39.15  ? 21  TRP   A O   1 
ATOM   164  C CB  . TRP   A 1 22 ? 1.149   -21.456 0.811   1.00 41.26  ? 21  TRP   A CB  1 
ATOM   165  C CG  . TRP   A 1 22 ? 2.236   -22.486 0.894   1.00 35.49  ? 21  TRP   A CG  1 
ATOM   166  C CD1 . TRP   A 1 22 ? 3.566   -22.257 0.719   1.00 43.36  ? 21  TRP   A CD1 1 
ATOM   167  C CD2 . TRP   A 1 22 ? 2.109   -23.886 1.214   1.00 35.05  ? 21  TRP   A CD2 1 
ATOM   168  N NE1 . TRP   A 1 22 ? 4.275   -23.414 0.907   1.00 42.68  ? 21  TRP   A NE1 1 
ATOM   169  C CE2 . TRP   A 1 22 ? 3.411   -24.432 1.206   1.00 36.43  ? 21  TRP   A CE2 1 
ATOM   170  C CE3 . TRP   A 1 22 ? 1.033   -24.741 1.488   1.00 40.03  ? 21  TRP   A CE3 1 
ATOM   171  C CZ2 . TRP   A 1 22 ? 3.668   -25.782 1.460   1.00 40.29  ? 21  TRP   A CZ2 1 
ATOM   172  C CZ3 . TRP   A 1 22 ? 1.279   -26.083 1.719   1.00 41.99  ? 21  TRP   A CZ3 1 
ATOM   173  C CH2 . TRP   A 1 22 ? 2.585   -26.593 1.726   1.00 42.22  ? 21  TRP   A CH2 1 
ATOM   174  N N   . PRO   A 1 23 ? 3.359   -19.421 2.534   1.00 35.28  ? 22  PRO   A N   1 
ATOM   175  C CA  . PRO   A 1 23 ? 4.451   -18.442 2.396   1.00 35.62  ? 22  PRO   A CA  1 
ATOM   176  C C   . PRO   A 1 23 ? 4.981   -18.427 0.967   1.00 29.34  ? 22  PRO   A C   1 
ATOM   177  O O   . PRO   A 1 23 ? 5.288   -19.471 0.421   1.00 31.82  ? 22  PRO   A O   1 
ATOM   178  C CB  . PRO   A 1 23 ? 5.533   -18.907 3.385   1.00 29.31  ? 22  PRO   A CB  1 
ATOM   179  C CG  . PRO   A 1 23 ? 5.177   -20.337 3.669   1.00 31.62  ? 22  PRO   A CG  1 
ATOM   180  C CD  . PRO   A 1 23 ? 3.659   -20.411 3.573   1.00 33.16  ? 22  PRO   A CD  1 
ATOM   181  N N   . ALA   A 1 24 ? 5.037   -17.235 0.391   1.00 30.06  ? 23  ALA   A N   1 
ATOM   182  C CA  . ALA   A 1 24 ? 5.432   -17.059 -0.996  1.00 32.41  ? 23  ALA   A CA  1 
ATOM   183  C C   . ALA   A 1 24 ? 5.997   -15.649 -1.231  1.00 31.60  ? 23  ALA   A C   1 
ATOM   184  O O   . ALA   A 1 24 ? 6.207   -14.861 -0.309  1.00 28.10  ? 23  ALA   A O   1 
ATOM   185  C CB  . ALA   A 1 24 ? 4.267   -17.380 -1.910  1.00 30.76  ? 23  ALA   A CB  1 
ATOM   186  N N   . ARG   A 1 25 ? 6.321   -15.378 -2.496  1.00 31.09  ? 24  ARG   A N   1 
ATOM   187  C CA  . ARG   A 1 25 ? 6.903   -14.134 -2.945  1.00 33.21  ? 24  ARG   A CA  1 
ATOM   188  C C   . ARG   A 1 25 ? 6.383   -13.896 -4.366  1.00 37.41  ? 24  ARG   A C   1 
ATOM   189  O O   . ARG   A 1 25 ? 6.007   -14.855 -5.043  1.00 32.02  ? 24  ARG   A O   1 
ATOM   190  C CB  . ARG   A 1 25 ? 8.431   -14.212 -2.853  1.00 29.80  ? 24  ARG   A CB  1 
ATOM   191  C CG  . ARG   A 1 25 ? 9.169   -15.076 -3.863  1.00 30.67  ? 24  ARG   A CG  1 
ATOM   192  C CD  . ARG   A 1 25 ? 10.656  -14.724 -3.886  1.00 29.46  ? 24  ARG   A CD  1 
ATOM   193  N NE  . ARG   A 1 25 ? 11.458  -15.460 -4.870  1.00 29.54  ? 24  ARG   A NE  1 
ATOM   194  C CZ  . ARG   A 1 25 ? 12.595  -16.152 -4.663  1.00 37.53  ? 24  ARG   A CZ  1 
ATOM   195  N NH1 . ARG   A 1 25 ? 13.230  -16.116 -3.505  1.00 37.90  ? 24  ARG   A NH1 1 
ATOM   196  N NH2 . ARG   A 1 25 ? 13.101  -16.919 -5.612  1.00 35.98  ? 24  ARG   A NH2 1 
ATOM   197  N N   . ILE   A 1 26 ? 6.288   -12.618 -4.762  1.00 33.42  ? 25  ILE   A N   1 
ATOM   198  C CA  . ILE   A 1 26 ? 6.037   -12.269 -6.148  1.00 36.04  ? 25  ILE   A CA  1 
ATOM   199  C C   . ILE   A 1 26 ? 7.371   -12.423 -6.862  1.00 32.15  ? 25  ILE   A C   1 
ATOM   200  O O   . ILE   A 1 26 ? 8.357   -11.834 -6.457  1.00 34.87  ? 25  ILE   A O   1 
ATOM   201  C CB  . ILE   A 1 26 ? 5.487   -10.835 -6.282  1.00 34.42  ? 25  ILE   A CB  1 
ATOM   202  C CG1 . ILE   A 1 26 ? 4.348   -10.582 -5.312  1.00 36.26  ? 25  ILE   A CG1 1 
ATOM   203  C CG2 . ILE   A 1 26 ? 5.062   -10.528 -7.726  1.00 34.90  ? 25  ILE   A CG2 1 
ATOM   204  C CD1 . ILE   A 1 26 ? 2.965   -10.772 -5.884  1.00 36.72  ? 25  ILE   A CD1 1 
ATOM   205  N N   . ASP   A 1 27 ? 7.423   -13.271 -7.875  1.00 38.41  ? 26  ASP   A N   1 
ATOM   206  C CA  . ASP   A 1 27 ? 8.686   -13.418 -8.584  1.00 42.26  ? 26  ASP   A CA  1 
ATOM   207  C C   . ASP   A 1 27 ? 8.799   -12.388 -9.694  1.00 43.60  ? 26  ASP   A C   1 
ATOM   208  O O   . ASP   A 1 27 ? 7.801   -11.787 -10.067 1.00 42.44  ? 26  ASP   A O   1 
ATOM   209  C CB  . ASP   A 1 27 ? 8.878   -14.811 -9.159  1.00 37.91  ? 26  ASP   A CB  1 
ATOM   210  C CG  . ASP   A 1 27 ? 9.768   -15.689 -8.314  1.00 38.77  ? 26  ASP   A CG  1 
ATOM   211  O OD1 . ASP   A 1 27 ? 10.310  -15.150 -7.324  1.00 40.74  ? 26  ASP   A OD1 1 
ATOM   212  O OD2 . ASP   A 1 27 ? 9.871   -16.884 -8.636  1.00 38.43  ? 26  ASP   A OD2 1 
ATOM   213  N N   . ASP   A 1 28 ? 10.029  -12.206 -10.197 1.00 47.40  ? 27  ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 28 ? 10.239  -11.583 -11.492 1.00 49.11  ? 27  ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 28 ? 10.007  -12.615 -12.580 1.00 46.32  ? 27  ASP   A C   1 
ATOM   216  O O   . ASP   A 1 28 ? 10.179  -13.810 -12.360 1.00 50.09  ? 27  ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 28 ? 11.647  -11.038 -11.660 1.00 50.27  ? 27  ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 28 ? 11.989  -9.893  -10.727 1.00 63.75  ? 27  ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 28 ? 11.949  -8.727  -11.188 1.00 59.96  ? 27  ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 28 ? 12.278  -10.186 -9.545  1.00 66.42  ? 27  ASP   A OD2 1 
ATOM   221  N N   . ILE   A 1 29 ? 9.635   -12.129 -13.760 1.00 50.14  ? 28  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 29 ? 9.738   -12.948 -14.955 1.00 50.46  ? 28  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 29 ? 11.133  -12.738 -15.531 1.00 53.85  ? 28  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 29 ? 11.509  -11.593 -15.785 1.00 52.03  ? 28  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 29 ? 8.650   -12.522 -15.947 1.00 55.90  ? 28  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 29 ? 7.269   -12.730 -15.319 1.00 56.47  ? 28  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 29 ? 8.803   -13.263 -17.277 1.00 49.65  ? 28  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 29 ? 6.195   -11.828 -15.891 1.00 65.99  ? 28  ILE   A CD1 1 
ATOM   229  N N   . ALA   A 1 30 ? 11.896  -13.835 -15.670 1.00 48.63  ? 29  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30 ? 13.211  -13.802 -16.298 1.00 46.86  ? 29  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30 ? 13.070  -13.657 -17.813 1.00 42.99  ? 29  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30 ? 12.034  -13.933 -18.409 1.00 36.40  ? 29  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30 ? 14.013  -15.038 -15.950 1.00 45.56  ? 29  ALA   A CB  1 
ATOM   234  N N   . ASP   A 1 31 ? 14.135  -13.176 -18.432 1.00 44.74  ? 30  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 31 ? 14.123  -12.974 -19.863 1.00 40.58  ? 30  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 31 ? 13.782  -14.299 -20.528 1.00 38.70  ? 30  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 31 ? 14.414  -15.317 -20.228 1.00 38.31  ? 30  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 31 ? 15.464  -12.432 -20.316 1.00 38.58  ? 30  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 31 ? 15.660  -10.953 -20.068 1.00 43.49  ? 30  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 31 ? 14.673  -10.211 -20.184 1.00 51.25  ? 30  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 31 ? 16.811  -10.551 -19.832 1.00 47.34  ? 30  ASP   A OD2 1 
ATOM   242  N N   . GLY   A 1 32 ? 12.771  -14.283 -21.407 1.00 38.18  ? 31  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 32 ? 12.499  -15.450 -22.238 1.00 43.95  ? 31  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 32 ? 11.656  -16.538 -21.564 1.00 43.36  ? 31  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 32 ? 11.290  -17.512 -22.213 1.00 40.50  ? 31  GLY   A O   1 
ATOM   246  N N   . ALA   A 1 33 ? 11.342  -16.348 -20.277 1.00 41.31  ? 32  ALA   A N   1 
ATOM   247  C CA  . ALA   A 1 33 ? 10.455  -17.188 -19.488 1.00 38.17  ? 32  ALA   A CA  1 
ATOM   248  C C   . ALA   A 1 33 ? 8.992   -16.816 -19.763 1.00 41.53  ? 32  ALA   A C   1 
ATOM   249  O O   . ALA   A 1 33 ? 8.683   -15.668 -20.101 1.00 39.79  ? 32  ALA   A O   1 
ATOM   250  C CB  . ALA   A 1 33 ? 10.827  -16.987 -18.017 1.00 33.48  ? 32  ALA   A CB  1 
ATOM   251  N N   . VAL   A 1 34 ? 8.081   -17.782 -19.556 1.00 42.18  ? 33  VAL   A N   1 
ATOM   252  C CA  . VAL   A 1 34 ? 6.647   -17.619 -19.760 1.00 40.03  ? 33  VAL   A CA  1 
ATOM   253  C C   . VAL   A 1 34 ? 6.076   -16.522 -18.857 1.00 41.39  ? 33  VAL   A C   1 
ATOM   254  O O   . VAL   A 1 34 ? 6.376   -16.461 -17.660 1.00 42.88  ? 33  VAL   A O   1 
ATOM   255  C CB  . VAL   A 1 34 ? 5.939   -18.967 -19.526 1.00 49.37  ? 33  VAL   A CB  1 
ATOM   256  C CG1 . VAL   A 1 34 ? 4.426   -18.871 -19.719 1.00 52.99  ? 33  VAL   A CG1 1 
ATOM   257  C CG2 . VAL   A 1 34 ? 6.533   -20.084 -20.382 1.00 46.70  ? 33  VAL   A CG2 1 
ATOM   258  N N   . LYS   A 1 35 ? 5.235   -15.665 -19.449 1.00 35.07  ? 34  LYS   A N   1 
ATOM   259  C CA  . LYS   A 1 35 ? 4.555   -14.574 -18.763 1.00 44.60  ? 34  LYS   A CA  1 
ATOM   260  C C   . LYS   A 1 35 ? 3.218   -15.043 -18.193 1.00 48.75  ? 34  LYS   A C   1 
ATOM   261  O O   . LYS   A 1 35 ? 2.532   -15.850 -18.795 1.00 49.87  ? 34  LYS   A O   1 
ATOM   262  C CB  . LYS   A 1 35 ? 4.268   -13.355 -19.653 1.00 43.28  ? 34  LYS   A CB  1 
ATOM   263  C CG  . LYS   A 1 35 ? 5.483   -12.465 -19.916 1.00 44.71  ? 34  LYS   A CG  1 
ATOM   264  C CD  . LYS   A 1 35 ? 5.243   -11.436 -21.013 1.00 44.37  ? 34  LYS   A CD  1 
ATOM   265  C CE  . LYS   A 1 35 ? 5.139   -12.038 -22.396 1.00 49.41  ? 34  LYS   A CE  1 
ATOM   266  N NZ  . LYS   A 1 35 ? 4.995   -10.991 -23.405 1.00 43.27  ? 34  LYS   A NZ  1 
ATOM   267  N N   . PRO   A 1 36 ? 2.801   -14.548 -17.009 1.00 50.83  ? 35  PRO   A N   1 
ATOM   268  C CA  . PRO   A 1 36 ? 1.522   -14.944 -16.439 1.00 50.53  ? 35  PRO   A CA  1 
ATOM   269  C C   . PRO   A 1 36 ? 0.416   -14.287 -17.258 1.00 58.21  ? 35  PRO   A C   1 
ATOM   270  O O   . PRO   A 1 36 ? 0.649   -13.282 -17.926 1.00 58.07  ? 35  PRO   A O   1 
ATOM   271  C CB  . PRO   A 1 36 ? 1.583   -14.405 -15.000 1.00 51.37  ? 35  PRO   A CB  1 
ATOM   272  C CG  . PRO   A 1 36 ? 2.595   -13.294 -15.038 1.00 51.35  ? 35  PRO   A CG  1 
ATOM   273  C CD  . PRO   A 1 36 ? 3.548   -13.603 -16.166 1.00 48.27  ? 35  PRO   A CD  1 
ATOM   274  N N   . PRO   A 1 37 ? -0.816  -14.845 -17.246 1.00 56.07  ? 36  PRO   A N   1 
ATOM   275  C CA  . PRO   A 1 37 ? -1.990  -14.141 -17.770 1.00 57.12  ? 36  PRO   A CA  1 
ATOM   276  C C   . PRO   A 1 37 ? -2.105  -12.703 -17.280 1.00 58.19  ? 36  PRO   A C   1 
ATOM   277  O O   . PRO   A 1 37 ? -1.552  -12.354 -16.236 1.00 59.56  ? 36  PRO   A O   1 
ATOM   278  C CB  . PRO   A 1 37 ? -3.171  -14.998 -17.271 1.00 54.34  ? 36  PRO   A CB  1 
ATOM   279  C CG  . PRO   A 1 37 ? -2.591  -16.395 -17.196 1.00 55.11  ? 36  PRO   A CG  1 
ATOM   280  C CD  . PRO   A 1 37 ? -1.126  -16.210 -16.784 1.00 57.38  ? 36  PRO   A CD  1 
ATOM   281  N N   . PRO   A 1 38 ? -2.856  -11.845 -18.011 1.00 61.67  ? 37  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 38 ? -3.151  -10.485 -17.557 1.00 59.46  ? 37  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 38 ? -3.773  -10.489 -16.159 1.00 57.75  ? 37  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 38 ? -4.581  -11.357 -15.837 1.00 56.28  ? 37  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 38 ? -4.129  -9.979  -18.642 1.00 60.37  ? 37  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 38 ? -4.701  -11.244 -19.259 1.00 57.96  ? 37  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 38 ? -3.492  -12.161 -19.304 1.00 64.57  ? 37  PRO   A CD  1 
ATOM   288  N N   . ASN   A 1 39 ? -3.373  -9.512  -15.339 1.00 53.84  ? 38  ASN   A N   1 
ATOM   289  C CA  . ASN   A 1 39 ? -3.807  -9.351  -13.957 1.00 55.64  ? 38  ASN   A CA  1 
ATOM   290  C C   . ASN   A 1 39 ? -3.398  -10.522 -13.064 1.00 47.59  ? 38  ASN   A C   1 
ATOM   291  O O   . ASN   A 1 39 ? -3.873  -10.605 -11.938 1.00 54.35  ? 38  ASN   A O   1 
ATOM   292  C CB  . ASN   A 1 39 ? -5.267  -8.919  -13.857 1.00 66.35  ? 38  ASN   A CB  1 
ATOM   293  C CG  . ASN   A 1 39 ? -5.490  -7.609  -14.572 1.00 67.95  ? 38  ASN   A CG  1 
ATOM   294  O OD1 . ASN   A 1 39 ? -5.197  -6.547  -14.014 1.00 71.27  ? 38  ASN   A OD1 1 
ATOM   295  N ND2 . ASN   A 1 39 ? -5.978  -7.665  -15.802 1.00 63.04  ? 38  ASN   A ND2 1 
ATOM   296  N N   . LYS   A 1 40 ? -2.496  -11.391 -13.542 1.00 42.12  ? 39  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 40 ? -1.892  -12.414 -12.693 1.00 43.05  ? 39  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 40 ? -0.420  -12.094 -12.403 1.00 44.79  ? 39  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 40 ? 0.259   -11.404 -13.166 1.00 43.99  ? 39  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 40 ? -2.122  -13.849 -13.188 1.00 39.03  ? 39  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 40 ? -3.584  -14.281 -13.401 1.00 39.84  ? 39  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 40 ? -4.503  -14.075 -12.199 1.00 41.73  ? 39  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 40 ? -5.948  -14.418 -12.514 1.00 44.63  ? 39  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 40 ? -6.172  -15.868 -12.638 1.00 34.23  ? 39  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 41 ? 0.044   -12.577 -11.244 1.00 41.58  ? 40  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 41 ? 1.425   -12.439 -10.816 1.00 36.90  ? 40  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 41 ? 1.993   -13.844 -10.726 1.00 33.16  ? 40  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 41 ? 1.280   -14.773 -10.349 1.00 40.21  ? 40  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 41 ? 1.568   -11.663 -9.497  1.00 34.06  ? 40  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 41 ? 1.080   -10.224 -9.564  1.00 30.32  ? 40  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 41 ? -0.286  -9.939  -9.514  1.00 39.95  ? 40  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 41 ? 1.958   -9.146  -9.679  1.00 32.55  ? 40  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 41 ? -0.755  -8.633  -9.605  1.00 32.56  ? 40  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 41 ? 1.502   -7.832  -9.759  1.00 29.89  ? 40  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 41 ? 0.141   -7.590  -9.732  1.00 31.99  ? 40  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 41 ? -0.375  -6.333  -9.766  1.00 44.26  ? 40  TYR   A OH  1 
ATOM   317  N N   . PRO   A 1 42 ? 3.272   -14.059 -11.102 1.00 34.33  ? 41  PRO   A N   1 
ATOM   318  C CA  . PRO   A 1 42 ? 3.916   -15.359 -10.876 1.00 31.31  ? 41  PRO   A CA  1 
ATOM   319  C C   . PRO   A 1 42 ? 4.260   -15.446 -9.385  1.00 29.47  ? 41  PRO   A C   1 
ATOM   320  O O   . PRO   A 1 42 ? 4.926   -14.579 -8.847  1.00 31.87  ? 41  PRO   A O   1 
ATOM   321  C CB  . PRO   A 1 42 ? 5.138   -15.240 -11.733 1.00 32.86  ? 41  PRO   A CB  1 
ATOM   322  C CG  . PRO   A 1 42 ? 5.491   -13.782 -11.611 1.00 34.17  ? 41  PRO   A CG  1 
ATOM   323  C CD  . PRO   A 1 42 ? 4.161   -13.054 -11.699 1.00 35.12  ? 41  PRO   A CD  1 
ATOM   324  N N   . ILE   A 1 43 ? 3.752   -16.470 -8.708  1.00 30.63  ? 42  ILE   A N   1 
ATOM   325  C CA  . ILE   A 1 43 ? 4.014   -16.614 -7.284  1.00 30.01  ? 42  ILE   A CA  1 
ATOM   326  C C   . ILE   A 1 43 ? 4.902   -17.846 -7.054  1.00 32.42  ? 42  ILE   A C   1 
ATOM   327  O O   . ILE   A 1 43 ? 4.546   -18.950 -7.453  1.00 37.40  ? 42  ILE   A O   1 
ATOM   328  C CB  . ILE   A 1 43 ? 2.711   -16.712 -6.474  1.00 28.04  ? 42  ILE   A CB  1 
ATOM   329  C CG1 . ILE   A 1 43 ? 1.621   -15.630 -6.844  1.00 27.27  ? 42  ILE   A CG1 1 
ATOM   330  C CG2 . ILE   A 1 43 ? 3.042   -16.763 -4.970  1.00 25.45  ? 42  ILE   A CG2 1 
ATOM   331  C CD1 . ILE   A 1 43 ? 2.066   -14.184 -6.672  1.00 30.02  ? 42  ILE   A CD1 1 
ATOM   332  N N   . PHE   A 1 44 ? 6.056   -17.652 -6.407  1.00 28.54  ? 43  PHE   A N   1 
ATOM   333  C CA  . PHE   A 1 44 ? 6.952   -18.727 -6.024  1.00 30.62  ? 43  PHE   A CA  1 
ATOM   334  C C   . PHE   A 1 44 ? 6.628   -19.075 -4.569  1.00 38.89  ? 43  PHE   A C   1 
ATOM   335  O O   . PHE   A 1 44 ? 6.580   -18.200 -3.694  1.00 32.33  ? 43  PHE   A O   1 
ATOM   336  C CB  . PHE   A 1 44 ? 8.400   -18.244 -6.192  1.00 32.34  ? 43  PHE   A CB  1 
ATOM   337  C CG  . PHE   A 1 44 ? 9.443   -19.242 -5.694  1.00 35.72  ? 43  PHE   A CG  1 
ATOM   338  C CD1 . PHE   A 1 44 ? 9.954   -20.222 -6.538  1.00 32.78  ? 43  PHE   A CD1 1 
ATOM   339  C CD2 . PHE   A 1 44 ? 9.878   -19.223 -4.370  1.00 31.74  ? 43  PHE   A CD2 1 
ATOM   340  C CE1 . PHE   A 1 44 ? 10.862  -21.158 -6.064  1.00 38.47  ? 43  PHE   A CE1 1 
ATOM   341  C CE2 . PHE   A 1 44 ? 10.810  -20.134 -3.911  1.00 33.87  ? 43  PHE   A CE2 1 
ATOM   342  C CZ  . PHE   A 1 44 ? 11.294  -21.108 -4.754  1.00 40.19  ? 43  PHE   A CZ  1 
ATOM   343  N N   . PHE   A 1 45 ? 6.357   -20.367 -4.341  1.00 39.34  ? 44  PHE   A N   1 
ATOM   344  C CA  . PHE   A 1 45 ? 5.909   -20.829 -3.046  1.00 34.93  ? 44  PHE   A CA  1 
ATOM   345  C C   . PHE   A 1 45 ? 7.146   -21.364 -2.349  1.00 40.16  ? 44  PHE   A C   1 
ATOM   346  O O   . PHE   A 1 45 ? 7.789   -22.285 -2.864  1.00 39.47  ? 44  PHE   A O   1 
ATOM   347  C CB  . PHE   A 1 45 ? 4.852   -21.936 -3.193  1.00 34.37  ? 44  PHE   A CB  1 
ATOM   348  C CG  . PHE   A 1 45 ? 3.511   -21.482 -3.749  1.00 41.14  ? 44  PHE   A CG  1 
ATOM   349  C CD1 . PHE   A 1 45 ? 3.298   -21.404 -5.131  1.00 38.67  ? 44  PHE   A CD1 1 
ATOM   350  C CD2 . PHE   A 1 45 ? 2.467   -21.141 -2.890  1.00 39.79  ? 44  PHE   A CD2 1 
ATOM   351  C CE1 . PHE   A 1 45 ? 2.083   -20.986 -5.644  1.00 38.94  ? 44  PHE   A CE1 1 
ATOM   352  C CE2 . PHE   A 1 45 ? 1.259   -20.704 -3.407  1.00 42.06  ? 44  PHE   A CE2 1 
ATOM   353  C CZ  . PHE   A 1 45 ? 1.070   -20.625 -4.778  1.00 44.52  ? 44  PHE   A CZ  1 
ATOM   354  N N   . PHE   A 1 46 ? 7.449   -20.799 -1.173  1.00 39.81  ? 45  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 46 ? 8.561   -21.311 -0.390  1.00 39.19  ? 45  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 46 ? 8.288   -22.747 0.018   1.00 37.92  ? 45  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 46 ? 7.126   -23.134 0.161   1.00 38.29  ? 45  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 46 ? 8.803   -20.484 0.869   1.00 38.85  ? 45  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 46 ? 9.246   -19.102 0.433   1.00 33.75  ? 45  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 46 ? 10.491  -18.911 -0.158  1.00 34.65  ? 45  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 46 ? 8.416   -18.004 0.615   1.00 30.84  ? 45  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 46 ? 10.908  -17.641 -0.526  1.00 31.07  ? 45  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 46 ? 8.842   -16.744 0.228   1.00 33.81  ? 45  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 46 ? 10.080  -16.562 -0.344  1.00 30.99  ? 45  PHE   A CZ  1 
ATOM   365  N N   . GLY   A 1 47 ? 9.376   -23.504 0.204   1.00 36.11  ? 46  GLY   A N   1 
ATOM   366  C CA  . GLY   A 1 47 ? 9.293   -24.876 0.669   1.00 39.03  ? 46  GLY   A CA  1 
ATOM   367  C C   . GLY   A 1 47 ? 9.086   -25.818 -0.512  1.00 41.45  ? 46  GLY   A C   1 
ATOM   368  O O   . GLY   A 1 47 ? 9.943   -26.637 -0.805  1.00 46.27  ? 46  GLY   A O   1 
ATOM   369  N N   . THR   A 1 48 ? 7.947   -25.686 -1.192  1.00 46.49  ? 47  THR   A N   1 
ATOM   370  C CA  . THR   A 1 48 ? 7.622   -26.536 -2.328  1.00 50.23  ? 47  THR   A CA  1 
ATOM   371  C C   . THR   A 1 48 ? 8.443   -26.101 -3.540  1.00 47.72  ? 47  THR   A C   1 
ATOM   372  O O   . THR   A 1 48 ? 8.687   -26.910 -4.436  1.00 57.70  ? 47  THR   A O   1 
ATOM   373  C CB  . THR   A 1 48 ? 6.120   -26.479 -2.618  1.00 46.54  ? 47  THR   A CB  1 
ATOM   374  O OG1 . THR   A 1 48 ? 5.803   -25.134 -2.997  1.00 48.10  ? 47  THR   A OG1 1 
ATOM   375  C CG2 . THR   A 1 48 ? 5.297   -26.996 -1.453  1.00 44.96  ? 47  THR   A CG2 1 
ATOM   376  N N   . HIS   A 1 49 ? 8.842   -24.821 -3.539  1.00 38.92  ? 48  HIS   A N   1 
ATOM   377  C CA  . HIS   A 1 49 ? 9.466   -24.146 -4.661  1.00 42.06  ? 48  HIS   A CA  1 
ATOM   378  C C   . HIS   A 1 49 ? 8.700   -24.372 -5.959  1.00 44.78  ? 48  HIS   A C   1 
ATOM   379  O O   . HIS   A 1 49 ? 9.336   -24.582 -6.987  1.00 47.11  ? 48  HIS   A O   1 
ATOM   380  C CB  . HIS   A 1 49 ? 10.927  -24.561 -4.867  1.00 45.18  ? 48  HIS   A CB  1 
ATOM   381  C CG  . HIS   A 1 49 ? 11.707  -24.619 -3.602  1.00 49.40  ? 48  HIS   A CG  1 
ATOM   382  N ND1 . HIS   A 1 49 ? 12.286  -25.786 -3.157  1.00 47.06  ? 48  HIS   A ND1 1 
ATOM   383  C CD2 . HIS   A 1 49 ? 11.928  -23.700 -2.663  1.00 49.35  ? 48  HIS   A CD2 1 
ATOM   384  C CE1 . HIS   A 1 49 ? 12.866  -25.559 -1.994  1.00 49.80  ? 48  HIS   A CE1 1 
ATOM   385  N NE2 . HIS   A 1 49 ? 12.676  -24.292 -1.688  1.00 55.76  ? 48  HIS   A NE2 1 
ATOM   386  N N   . GLU   A 1 50 ? 7.365   -24.243 -5.921  1.00 50.95  ? 49  GLU   A N   1 
ATOM   387  C CA  . GLU   A 1 50 ? 6.539   -24.339 -7.118  1.00 49.01  ? 49  GLU   A CA  1 
ATOM   388  C C   . GLU   A 1 50 ? 5.993   -22.964 -7.471  1.00 44.12  ? 49  GLU   A C   1 
ATOM   389  O O   . GLU   A 1 50 ? 5.904   -22.118 -6.582  1.00 43.90  ? 49  GLU   A O   1 
ATOM   390  C CB  . GLU   A 1 50 ? 5.390   -25.316 -6.880  1.00 51.86  ? 49  GLU   A CB  1 
ATOM   391  C CG  . GLU   A 1 50 ? 5.866   -26.761 -6.784  1.00 58.28  ? 49  GLU   A CG  1 
ATOM   392  C CD  . GLU   A 1 50 ? 4.890   -27.708 -6.116  1.00 69.17  ? 49  GLU   A CD  1 
ATOM   393  O OE1 . GLU   A 1 50 ? 3.805   -27.263 -5.674  1.00 75.22  ? 49  GLU   A OE1 1 
ATOM   394  O OE2 . GLU   A 1 50 ? 5.230   -28.905 -6.019  1.00 75.69  ? 49  GLU   A OE2 1 
ATOM   395  N N   . THR   A 1 51 ? 5.641   -22.768 -8.764  1.00 43.24  ? 50  THR   A N   1 
ATOM   396  C CA  . THR   A 1 51 ? 5.040   -21.528 -9.245  1.00 43.31  ? 50  THR   A CA  1 
ATOM   397  C C   . THR   A 1 51 ? 3.585   -21.736 -9.672  1.00 42.71  ? 50  THR   A C   1 
ATOM   398  O O   . THR   A 1 51 ? 3.290   -22.621 -10.461 1.00 51.44  ? 50  THR   A O   1 
ATOM   399  C CB  . THR   A 1 51 ? 5.843   -20.878 -10.372 1.00 47.23  ? 50  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 51 ? 7.103   -20.490 -9.843  1.00 46.18  ? 50  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 51 ? 5.185   -19.605 -10.888 1.00 43.82  ? 50  THR   A CG2 1 
ATOM   402  N N   . ALA   A 1 52 ? 2.685   -20.882 -9.176  1.00 38.06  ? 51  ALA   A N   1 
ATOM   403  C CA  . ALA   A 1 52 ? 1.395   -20.684 -9.816  1.00 39.49  ? 51  ALA   A CA  1 
ATOM   404  C C   . ALA   A 1 52 ? 1.224   -19.212 -10.156 1.00 38.32  ? 51  ALA   A C   1 
ATOM   405  O O   . ALA   A 1 52 ? 2.031   -18.376 -9.747  1.00 37.88  ? 51  ALA   A O   1 
ATOM   406  C CB  . ALA   A 1 52 ? 0.263   -21.179 -8.945  1.00 40.63  ? 51  ALA   A CB  1 
ATOM   407  N N   . PHE   A 1 53 ? 0.192   -18.933 -10.952 1.00 37.04  ? 52  PHE   A N   1 
ATOM   408  C CA  . PHE   A 1 53 ? -0.255  -17.585 -11.270 1.00 42.37  ? 52  PHE   A CA  1 
ATOM   409  C C   . PHE   A 1 53 ? -1.504  -17.283 -10.449 1.00 41.50  ? 52  PHE   A C   1 
ATOM   410  O O   . PHE   A 1 53 ? -2.436  -18.077 -10.451 1.00 47.77  ? 52  PHE   A O   1 
ATOM   411  C CB  . PHE   A 1 53 ? -0.530  -17.517 -12.779 1.00 41.67  ? 52  PHE   A CB  1 
ATOM   412  C CG  . PHE   A 1 53 ? 0.696   -17.802 -13.641 1.00 50.15  ? 52  PHE   A CG  1 
ATOM   413  C CD1 . PHE   A 1 53 ? 1.861   -17.048 -13.505 1.00 48.55  ? 52  PHE   A CD1 1 
ATOM   414  C CD2 . PHE   A 1 53 ? 0.693   -18.845 -14.568 1.00 51.46  ? 52  PHE   A CD2 1 
ATOM   415  C CE1 . PHE   A 1 53 ? 2.972   -17.313 -14.295 1.00 55.22  ? 52  PHE   A CE1 1 
ATOM   416  C CE2 . PHE   A 1 53 ? 1.807   -19.101 -15.363 1.00 51.79  ? 52  PHE   A CE2 1 
ATOM   417  C CZ  . PHE   A 1 53 ? 2.944   -18.340 -15.222 1.00 51.51  ? 52  PHE   A CZ  1 
ATOM   418  N N   . LEU   A 1 54 ? -1.506  -16.138 -9.759  1.00 42.26  ? 53  LEU   A N   1 
ATOM   419  C CA  . LEU   A 1 54 ? -2.566  -15.741 -8.841  1.00 40.71  ? 53  LEU   A CA  1 
ATOM   420  C C   . LEU   A 1 54 ? -2.809  -14.236 -8.952  1.00 36.99  ? 53  LEU   A C   1 
ATOM   421  O O   . LEU   A 1 54 ? -1.860  -13.465 -9.115  1.00 38.39  ? 53  LEU   A O   1 
ATOM   422  C CB  . LEU   A 1 54 ? -2.199  -16.096 -7.399  1.00 41.96  ? 53  LEU   A CB  1 
ATOM   423  C CG  . LEU   A 1 54 ? -2.045  -17.580 -7.061  1.00 45.81  ? 53  LEU   A CG  1 
ATOM   424  C CD1 . LEU   A 1 54 ? -1.554  -17.624 -5.629  1.00 50.97  ? 53  LEU   A CD1 1 
ATOM   425  C CD2 . LEU   A 1 54 ? -3.377  -18.299 -7.154  1.00 43.17  ? 53  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 55 ? -4.089  -13.843 -8.877  1.00 34.90  ? 54  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 55 ? -4.463  -12.444 -8.718  1.00 33.01  ? 54  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 55 ? -4.369  -12.016 -7.248  1.00 36.29  ? 54  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 55 ? -4.201  -12.857 -6.347  1.00 33.75  ? 54  GLY   A O   1 
ATOM   430  N N   . PRO   A 1 56 ? -4.436  -10.688 -6.981  1.00 35.53  ? 55  PRO   A N   1 
ATOM   431  C CA  . PRO   A 1 56 ? -4.436  -10.138 -5.619  1.00 31.90  ? 55  PRO   A CA  1 
ATOM   432  C C   . PRO   A 1 56 ? -5.407  -10.662 -4.560  1.00 34.76  ? 55  PRO   A C   1 
ATOM   433  O O   . PRO   A 1 56 ? -5.078  -10.632 -3.363  1.00 34.92  ? 55  PRO   A O   1 
ATOM   434  C CB  . PRO   A 1 56 ? -4.537  -8.597  -5.791  1.00 33.36  ? 55  PRO   A CB  1 
ATOM   435  C CG  . PRO   A 1 56 ? -4.173  -8.326  -7.248  1.00 33.17  ? 55  PRO   A CG  1 
ATOM   436  C CD  . PRO   A 1 56 ? -4.399  -9.639  -8.012  1.00 32.72  ? 55  PRO   A CD  1 
ATOM   437  N N   . LYS   A 1 57 ? -6.610  -11.084 -4.981  1.00 33.21  ? 56  LYS   A N   1 
ATOM   438  C CA  . LYS   A 1 57 ? -7.550  -11.702 -4.052  1.00 42.47  ? 56  LYS   A CA  1 
ATOM   439  C C   . LYS   A 1 57 ? -6.921  -12.879 -3.283  1.00 38.40  ? 56  LYS   A C   1 
ATOM   440  O O   . LYS   A 1 57 ? -7.334  -13.223 -2.175  1.00 36.57  ? 56  LYS   A O   1 
ATOM   441  C CB  . LYS   A 1 57 ? -8.782  -12.247 -4.788  1.00 45.30  ? 56  LYS   A CB  1 
ATOM   442  C CG  . LYS   A 1 57 ? -8.554  -13.468 -5.658  1.00 51.03  ? 56  LYS   A CG  1 
ATOM   443  C CD  . LYS   A 1 57 ? -9.870  -13.874 -6.316  1.00 64.83  ? 56  LYS   A CD  1 
ATOM   444  C CE  . LYS   A 1 57 ? -9.809  -15.071 -7.215  1.00 69.07  ? 56  LYS   A CE  1 
ATOM   445  N NZ  . LYS   A 1 57 ? -9.448  -16.272 -6.456  1.00 85.19  ? 56  LYS   A NZ  1 
ATOM   446  N N   . ASP   A 1 58 ? -5.912  -13.509 -3.867  1.00 30.66  ? 57  ASP   A N   1 
ATOM   447  C CA  . ASP   A 1 58 ? -5.317  -14.656 -3.219  1.00 33.38  ? 57  ASP   A CA  1 
ATOM   448  C C   . ASP   A 1 58 ? -4.038  -14.299 -2.451  1.00 33.79  ? 57  ASP   A C   1 
ATOM   449  O O   . ASP   A 1 58 ? -3.430  -15.181 -1.848  1.00 40.43  ? 57  ASP   A O   1 
ATOM   450  C CB  . ASP   A 1 58 ? -5.266  -15.809 -4.196  1.00 29.84  ? 57  ASP   A CB  1 
ATOM   451  C CG  . ASP   A 1 58 ? -6.642  -16.377 -4.525  1.00 33.63  ? 57  ASP   A CG  1 
ATOM   452  O OD1 . ASP   A 1 58 ? -7.506  -16.486 -3.540  1.00 18.18  ? 57  ASP   A OD1 1 
ATOM   453  O OD2 . ASP   A 1 58 ? -6.870  -16.650 -5.752  1.00 20.11  ? 57  ASP   A OD2 1 
ATOM   454  N N   . LEU   A 1 59 ? -3.654  -13.013 -2.441  1.00 28.69  ? 58  LEU   A N   1 
ATOM   455  C CA  . LEU   A 1 59 ? -2.315  -12.580 -2.020  1.00 27.50  ? 58  LEU   A CA  1 
ATOM   456  C C   . LEU   A 1 59 ? -2.424  -11.755 -0.738  1.00 26.08  ? 58  LEU   A C   1 
ATOM   457  O O   . LEU   A 1 59 ? -3.124  -10.726 -0.725  1.00 27.97  ? 58  LEU   A O   1 
ATOM   458  C CB  . LEU   A 1 59 ? -1.640  -11.792 -3.137  1.00 24.71  ? 58  LEU   A CB  1 
ATOM   459  C CG  . LEU   A 1 59 ? -1.523  -12.519 -4.487  1.00 26.89  ? 58  LEU   A CG  1 
ATOM   460  C CD1 . LEU   A 1 59 ? -1.005  -11.624 -5.599  1.00 25.81  ? 58  LEU   A CD1 1 
ATOM   461  C CD2 . LEU   A 1 59 ? -0.715  -13.835 -4.411  1.00 23.89  ? 58  LEU   A CD2 1 
ATOM   462  N N   . PHE   A 1 60 ? -1.818  -12.271 0.341   1.00 24.54  ? 59  PHE   A N   1 
ATOM   463  C CA  . PHE   A 1 60 ? -1.908  -11.662 1.670   1.00 27.32  ? 59  PHE   A CA  1 
ATOM   464  C C   . PHE   A 1 60 ? -0.527  -11.174 2.075   1.00 27.57  ? 59  PHE   A C   1 
ATOM   465  O O   . PHE   A 1 60 ? 0.381   -11.996 2.265   1.00 33.47  ? 59  PHE   A O   1 
ATOM   466  C CB  . PHE   A 1 60 ? -2.495  -12.584 2.738   1.00 28.64  ? 59  PHE   A CB  1 
ATOM   467  C CG  . PHE   A 1 60 ? -3.908  -13.053 2.398   1.00 36.66  ? 59  PHE   A CG  1 
ATOM   468  C CD1 . PHE   A 1 60 ? -4.147  -13.845 1.269   1.00 40.37  ? 59  PHE   A CD1 1 
ATOM   469  C CD2 . PHE   A 1 60 ? -4.993  -12.700 3.195   1.00 33.38  ? 59  PHE   A CD2 1 
ATOM   470  C CE1 . PHE   A 1 60 ? -5.432  -14.229 0.939   1.00 39.39  ? 59  PHE   A CE1 1 
ATOM   471  C CE2 . PHE   A 1 60 ? -6.273  -13.130 2.874   1.00 34.55  ? 59  PHE   A CE2 1 
ATOM   472  C CZ  . PHE   A 1 60 ? -6.489  -13.872 1.746   1.00 36.95  ? 59  PHE   A CZ  1 
ATOM   473  N N   . PRO   A 1 61 ? -0.307  -9.838  2.130   1.00 27.82  ? 60  PRO   A N   1 
ATOM   474  C CA  . PRO   A 1 61 ? 0.963   -9.272  2.592   1.00 31.25  ? 60  PRO   A CA  1 
ATOM   475  C C   . PRO   A 1 61 ? 1.467   -9.932  3.871   1.00 35.88  ? 60  PRO   A C   1 
ATOM   476  O O   . PRO   A 1 61 ? 0.685   -10.165 4.809   1.00 33.32  ? 60  PRO   A O   1 
ATOM   477  C CB  . PRO   A 1 61 ? 0.632   -7.765  2.803   1.00 31.56  ? 60  PRO   A CB  1 
ATOM   478  C CG  . PRO   A 1 61 ? -0.438  -7.507  1.737   1.00 36.56  ? 60  PRO   A CG  1 
ATOM   479  C CD  . PRO   A 1 61 ? -1.278  -8.782  1.742   1.00 30.47  ? 60  PRO   A CD  1 
ATOM   480  N N   . TYR   A 1 62 ? 2.778   -10.226 3.852   1.00 34.84  ? 61  TYR   A N   1 
ATOM   481  C CA  . TYR   A 1 62 ? 3.413   -11.089 4.828   1.00 34.99  ? 61  TYR   A CA  1 
ATOM   482  C C   . TYR   A 1 62 ? 3.438   -10.399 6.193   1.00 35.34  ? 61  TYR   A C   1 
ATOM   483  O O   . TYR   A 1 62 ? 3.115   -11.033 7.202   1.00 38.92  ? 61  TYR   A O   1 
ATOM   484  C CB  . TYR   A 1 62 ? 4.747   -11.665 4.323   1.00 40.33  ? 61  TYR   A CB  1 
ATOM   485  C CG  . TYR   A 1 62 ? 5.568   -12.331 5.420   1.00 36.02  ? 61  TYR   A CG  1 
ATOM   486  C CD1 . TYR   A 1 62 ? 5.334   -13.645 5.800   1.00 30.73  ? 61  TYR   A CD1 1 
ATOM   487  C CD2 . TYR   A 1 62 ? 6.533   -11.614 6.112   1.00 36.60  ? 61  TYR   A CD2 1 
ATOM   488  C CE1 . TYR   A 1 62 ? 6.074   -14.246 6.802   1.00 36.83  ? 61  TYR   A CE1 1 
ATOM   489  C CE2 . TYR   A 1 62 ? 7.277   -12.204 7.118   1.00 37.65  ? 61  TYR   A CE2 1 
ATOM   490  C CZ  . TYR   A 1 62 ? 7.039   -13.517 7.471   1.00 39.88  ? 61  TYR   A CZ  1 
ATOM   491  O OH  . TYR   A 1 62 ? 7.764   -14.066 8.481   1.00 44.38  ? 61  TYR   A OH  1 
ATOM   492  N N   . ASP   A 1 63 ? 3.807   -9.109  6.211   1.00 34.21  ? 62  ASP   A N   1 
ATOM   493  C CA  . ASP   A 1 63 ? 4.121   -8.470  7.471   1.00 36.36  ? 62  ASP   A CA  1 
ATOM   494  C C   . ASP   A 1 63 ? 2.883   -8.598  8.353   1.00 38.47  ? 62  ASP   A C   1 
ATOM   495  O O   . ASP   A 1 63 ? 2.977   -9.031  9.490   1.00 41.90  ? 62  ASP   A O   1 
ATOM   496  C CB  . ASP   A 1 63 ? 4.716   -7.085  7.260   1.00 39.88  ? 62  ASP   A CB  1 
ATOM   497  N N   . LYS   A 1 64 ? 1.720   -8.306  7.754   1.00 49.84  ? 63  LYS   A N   1 
ATOM   498  C CA  . LYS   A 1 64 ? 0.417   -8.133  8.385   1.00 46.64  ? 63  LYS   A CA  1 
ATOM   499  C C   . LYS   A 1 64 ? -0.268  -9.470  8.646   1.00 49.67  ? 63  LYS   A C   1 
ATOM   500  O O   . LYS   A 1 64 ? -1.182  -9.530  9.469   1.00 50.81  ? 63  LYS   A O   1 
ATOM   501  C CB  . LYS   A 1 64 ? -0.444  -7.316  7.410   1.00 46.55  ? 63  LYS   A CB  1 
ATOM   502  C CG  . LYS   A 1 64 ? -1.938  -7.215  7.710   1.00 52.60  ? 63  LYS   A CG  1 
ATOM   503  C CD  . LYS   A 1 64 ? -2.707  -6.340  6.728   1.00 49.79  ? 63  LYS   A CD  1 
ATOM   504  C CE  . LYS   A 1 64 ? -3.949  -5.822  7.351   1.00 48.29  ? 63  LYS   A CE  1 
ATOM   505  N NZ  . LYS   A 1 64 ? -4.968  -6.867  7.334   1.00 57.59  ? 63  LYS   A NZ  1 
ATOM   506  N N   . SER   A 1 65 ? 0.149   -10.523 7.934   1.00 42.35  ? 64  SER   A N   1 
ATOM   507  C CA  . SER   A 1 65 ? -0.623  -11.755 7.954   1.00 46.02  ? 64  SER   A CA  1 
ATOM   508  C C   . SER   A 1 65 ? 0.092   -12.882 8.697   1.00 47.10  ? 64  SER   A C   1 
ATOM   509  O O   . SER   A 1 65 ? -0.492  -13.943 8.898   1.00 48.56  ? 64  SER   A O   1 
ATOM   510  C CB  . SER   A 1 65 ? -0.975  -12.172 6.555   1.00 48.17  ? 64  SER   A CB  1 
ATOM   511  O OG  . SER   A 1 65 ? -1.829  -11.194 5.980   1.00 60.29  ? 64  SER   A OG  1 
ATOM   512  N N   . LYS   A 1 66 ? 1.345   -12.647 9.103   1.00 45.73  ? 65  LYS   A N   1 
ATOM   513  C CA  . LYS   A 1 66 ? 2.181   -13.708 9.637   1.00 45.29  ? 65  LYS   A CA  1 
ATOM   514  C C   . LYS   A 1 66 ? 1.714   -14.206 11.001  1.00 46.75  ? 65  LYS   A C   1 
ATOM   515  O O   . LYS   A 1 66 ? 1.952   -15.374 11.308  1.00 53.47  ? 65  LYS   A O   1 
ATOM   516  C CB  . LYS   A 1 66 ? 3.677   -13.385 9.712   1.00 49.27  ? 65  LYS   A CB  1 
ATOM   517  C CG  . LYS   A 1 66 ? 4.069   -12.088 10.379  1.00 51.51  ? 65  LYS   A CG  1 
ATOM   518  C CD  . LYS   A 1 66 ? 5.588   -12.110 10.474  1.00 60.63  ? 65  LYS   A CD  1 
ATOM   519  C CE  . LYS   A 1 66 ? 6.113   -10.875 11.127  1.00 65.72  ? 65  LYS   A CE  1 
ATOM   520  N NZ  . LYS   A 1 66 ? 6.107   -9.763  10.170  1.00 79.49  ? 65  LYS   A NZ  1 
ATOM   521  N N   A ASP   A 1 67 ? 1.075   -13.338 11.801  0.50 46.93  ? 66  ASP   A N   1 
ATOM   522  N N   B ASP   A 1 67 ? 1.076   -13.349 11.815  0.50 42.04  ? 66  ASP   A N   1 
ATOM   523  C CA  A ASP   A 1 67 ? 0.527   -13.750 13.086  0.50 49.99  ? 66  ASP   A CA  1 
ATOM   524  C CA  B ASP   A 1 67 ? 0.561   -13.837 13.089  0.50 41.01  ? 66  ASP   A CA  1 
ATOM   525  C C   A ASP   A 1 67 ? -0.592  -14.774 12.878  0.50 52.06  ? 66  ASP   A C   1 
ATOM   526  C C   B ASP   A 1 67 ? -0.557  -14.850 12.837  0.50 46.26  ? 66  ASP   A C   1 
ATOM   527  O O   A ASP   A 1 67 ? -0.723  -15.722 13.646  0.50 53.12  ? 66  ASP   A O   1 
ATOM   528  O O   B ASP   A 1 67 ? -0.648  -15.860 13.529  0.50 46.19  ? 66  ASP   A O   1 
ATOM   529  C CB  A ASP   A 1 67 ? 0.117   -12.560 13.939  0.50 56.30  ? 66  ASP   A CB  1 
ATOM   530  C CB  B ASP   A 1 67 ? 0.127   -12.736 14.040  0.50 37.99  ? 66  ASP   A CB  1 
ATOM   531  C CG  A ASP   A 1 67 ? 1.265   -11.687 14.432  0.50 64.49  ? 66  ASP   A CG  1 
ATOM   532  C CG  B ASP   A 1 67 ? 0.207   -13.103 15.517  0.50 35.35  ? 66  ASP   A CG  1 
ATOM   533  O OD1 A ASP   A 1 67 ? 2.433   -12.147 14.351  0.50 66.40  ? 66  ASP   A OD1 1 
ATOM   534  O OD1 B ASP   A 1 67 ? 1.233   -13.680 15.920  0.50 34.86  ? 66  ASP   A OD1 1 
ATOM   535  O OD2 A ASP   A 1 67 ? 0.987   -10.546 14.871  0.50 55.73  ? 66  ASP   A OD2 1 
ATOM   536  O OD2 B ASP   A 1 67 ? -0.738  -12.782 16.257  0.50 35.53  ? 66  ASP   A OD2 1 
ATOM   537  N N   . LYS   A 1 68 ? -1.362  -14.605 11.800  1.00 50.22  ? 67  LYS   A N   1 
ATOM   538  C CA  . LYS   A 1 68 ? -2.459  -15.505 11.491  1.00 55.23  ? 67  LYS   A CA  1 
ATOM   539  C C   . LYS   A 1 68 ? -1.964  -16.801 10.848  1.00 52.91  ? 67  LYS   A C   1 
ATOM   540  O O   . LYS   A 1 68 ? -2.551  -17.862 11.071  1.00 50.37  ? 67  LYS   A O   1 
ATOM   541  C CB  . LYS   A 1 68 ? -3.504  -14.783 10.631  1.00 58.69  ? 67  LYS   A CB  1 
ATOM   542  C CG  . LYS   A 1 68 ? -4.815  -15.552 10.436  1.00 63.35  ? 67  LYS   A CG  1 
ATOM   543  C CD  . LYS   A 1 68 ? -5.945  -14.611 10.019  1.00 69.43  ? 67  LYS   A CD  1 
ATOM   544  C CE  . LYS   A 1 68 ? -7.267  -15.269 9.773   1.00 67.06  ? 67  LYS   A CE  1 
ATOM   545  N NZ  . LYS   A 1 68 ? -8.332  -14.279 9.588   1.00 60.26  ? 67  LYS   A NZ  1 
ATOM   546  N N   . TYR   A 1 69 ? -0.910  -16.712 10.024  1.00 51.73  ? 68  TYR   A N   1 
ATOM   547  C CA  . TYR   A 1 69 ? -0.665  -17.741 9.019   1.00 47.00  ? 68  TYR   A CA  1 
ATOM   548  C C   . TYR   A 1 69 ? 0.725   -18.351 9.174   1.00 46.30  ? 68  TYR   A C   1 
ATOM   549  O O   . TYR   A 1 69 ? 0.960   -19.436 8.660   1.00 43.16  ? 68  TYR   A O   1 
ATOM   550  C CB  . TYR   A 1 69 ? -0.818  -17.207 7.590   1.00 49.27  ? 68  TYR   A CB  1 
ATOM   551  C CG  . TYR   A 1 69 ? -2.230  -16.793 7.195   1.00 49.92  ? 68  TYR   A CG  1 
ATOM   552  C CD1 . TYR   A 1 69 ? -3.336  -17.615 7.448   1.00 51.95  ? 68  TYR   A CD1 1 
ATOM   553  C CD2 . TYR   A 1 69 ? -2.460  -15.565 6.577   1.00 50.47  ? 68  TYR   A CD2 1 
ATOM   554  C CE1 . TYR   A 1 69 ? -4.625  -17.226 7.102   1.00 48.62  ? 68  TYR   A CE1 1 
ATOM   555  C CE2 . TYR   A 1 69 ? -3.743  -15.180 6.207   1.00 49.55  ? 68  TYR   A CE2 1 
ATOM   556  C CZ  . TYR   A 1 69 ? -4.828  -16.005 6.472   1.00 49.50  ? 68  TYR   A CZ  1 
ATOM   557  O OH  . TYR   A 1 69 ? -6.080  -15.580 6.108   1.00 50.97  ? 68  TYR   A OH  1 
ATOM   558  N N   . GLY   A 1 70 ? 1.630   -17.640 9.856   1.00 44.30  ? 69  GLY   A N   1 
ATOM   559  C CA  . GLY   A 1 70 ? 3.002   -18.079 10.018  1.00 42.45  ? 69  GLY   A CA  1 
ATOM   560  C C   . GLY   A 1 70 ? 3.129   -19.049 11.188  1.00 46.78  ? 69  GLY   A C   1 
ATOM   561  O O   . GLY   A 1 70 ? 3.995   -18.910 12.042  1.00 44.36  ? 69  GLY   A O   1 
ATOM   562  N N   . LYS   A 1 71 ? 2.240   -20.038 11.237  1.00 55.84  ? 70  LYS   A N   1 
ATOM   563  C CA  . LYS   A 1 71 ? 2.344   -21.076 12.255  1.00 53.41  ? 70  LYS   A CA  1 
ATOM   564  C C   . LYS   A 1 71 ? 2.557   -22.407 11.536  1.00 53.69  ? 70  LYS   A C   1 
ATOM   565  O O   . LYS   A 1 71 ? 2.206   -22.542 10.367  1.00 54.96  ? 70  LYS   A O   1 
ATOM   566  C CB  . LYS   A 1 71 ? 1.249   -20.912 13.319  1.00 55.10  ? 70  LYS   A CB  1 
ATOM   567  C CG  . LYS   A 1 71 ? 0.987   -19.453 13.762  1.00 60.97  ? 70  LYS   A CG  1 
ATOM   568  C CD  . LYS   A 1 71 ? 1.241   -19.030 15.211  1.00 63.51  ? 70  LYS   A CD  1 
ATOM   569  N N   . PRO   A 1 72 ? 3.258   -23.381 12.155  1.00 52.12  ? 71  PRO   A N   1 
ATOM   570  C CA  . PRO   A 1 72 ? 3.609   -24.625 11.469  1.00 47.82  ? 71  PRO   A CA  1 
ATOM   571  C C   . PRO   A 1 72 ? 2.403   -25.442 11.015  1.00 53.13  ? 71  PRO   A C   1 
ATOM   572  O O   . PRO   A 1 72 ? 1.290   -25.240 11.502  1.00 51.06  ? 71  PRO   A O   1 
ATOM   573  C CB  . PRO   A 1 72 ? 4.503   -25.405 12.447  1.00 51.56  ? 71  PRO   A CB  1 
ATOM   574  C CG  . PRO   A 1 72 ? 4.356   -24.687 13.782  1.00 52.54  ? 71  PRO   A CG  1 
ATOM   575  C CD  . PRO   A 1 72 ? 3.786   -23.300 13.526  1.00 53.72  ? 71  PRO   A CD  1 
ATOM   576  N N   . ASN   A 1 73 ? 2.658   -26.373 10.091  1.00 49.67  ? 72  ASN   A N   1 
ATOM   577  C CA  . ASN   A 1 73 ? 1.598   -27.092 9.411   1.00 56.47  ? 72  ASN   A CA  1 
ATOM   578  C C   . ASN   A 1 73 ? 2.129   -28.419 8.884   1.00 57.45  ? 72  ASN   A C   1 
ATOM   579  O O   . ASN   A 1 73 ? 3.264   -28.508 8.418   1.00 59.61  ? 72  ASN   A O   1 
ATOM   580  C CB  . ASN   A 1 73 ? 1.023   -26.276 8.258   1.00 54.12  ? 72  ASN   A CB  1 
ATOM   581  C CG  . ASN   A 1 73 ? -0.168  -26.957 7.637   1.00 50.06  ? 72  ASN   A CG  1 
ATOM   582  O OD1 . ASN   A 1 73 ? -0.102  -27.414 6.494   1.00 54.96  ? 72  ASN   A OD1 1 
ATOM   583  N ND2 . ASN   A 1 73 ? -1.249  -27.083 8.386   1.00 59.56  ? 72  ASN   A ND2 1 
ATOM   584  N N   . LYS   A 1 74 ? 1.255   -29.427 8.913   1.00 55.18  ? 73  LYS   A N   1 
ATOM   585  C CA  . LYS   A 1 74 ? 1.565   -30.773 8.465   1.00 58.86  ? 73  LYS   A CA  1 
ATOM   586  C C   . LYS   A 1 74 ? 2.076   -30.757 7.022   1.00 63.16  ? 73  LYS   A C   1 
ATOM   587  O O   . LYS   A 1 74 ? 2.946   -31.562 6.682   1.00 61.15  ? 73  LYS   A O   1 
ATOM   588  C CB  . LYS   A 1 74 ? 0.397   -31.748 8.696   1.00 68.11  ? 73  LYS   A CB  1 
ATOM   589  C CG  . LYS   A 1 74 ? -0.928  -31.472 7.979   1.00 64.16  ? 73  LYS   A CG  1 
ATOM   590  N N   . ARG   A 1 75 ? 1.585   -29.813 6.201   1.00 52.46  ? 74  ARG   A N   1 
ATOM   591  C CA  . ARG   A 1 75 ? 1.744   -29.914 4.753   1.00 51.85  ? 74  ARG   A CA  1 
ATOM   592  C C   . ARG   A 1 75 ? 3.212   -29.957 4.303   1.00 52.93  ? 74  ARG   A C   1 
ATOM   593  O O   . ARG   A 1 75 ? 4.075   -29.222 4.797   1.00 43.33  ? 74  ARG   A O   1 
ATOM   594  C CB  . ARG   A 1 75 ? 0.956   -28.849 3.987   1.00 53.83  ? 74  ARG   A CB  1 
ATOM   595  C CG  . ARG   A 1 75 ? -0.560  -28.876 4.069   1.00 55.79  ? 74  ARG   A CG  1 
ATOM   596  C CD  . ARG   A 1 75 ? -1.130  -30.139 3.440   1.00 56.42  ? 74  ARG   A CD  1 
ATOM   597  N NE  . ARG   A 1 75 ? -2.332  -29.792 2.676   1.00 63.08  ? 74  ARG   A NE  1 
ATOM   598  C CZ  . ARG   A 1 75 ? -3.444  -29.246 3.166   1.00 64.27  ? 74  ARG   A CZ  1 
ATOM   599  N NH1 . ARG   A 1 75 ? -4.398  -28.921 2.313   1.00 63.40  ? 74  ARG   A NH1 1 
ATOM   600  N NH2 . ARG   A 1 75 ? -3.599  -29.025 4.475   1.00 58.03  ? 74  ARG   A NH2 1 
ATOM   601  N N   . LYS   A 1 76 ? 3.460   -30.846 3.330   1.00 53.82  ? 75  LYS   A N   1 
ATOM   602  C CA  . LYS   A 1 76 ? 4.746   -31.050 2.680   1.00 53.52  ? 75  LYS   A CA  1 
ATOM   603  C C   . LYS   A 1 76 ? 5.258   -29.701 2.191   1.00 50.49  ? 75  LYS   A C   1 
ATOM   604  O O   . LYS   A 1 76 ? 4.611   -29.069 1.362   1.00 46.77  ? 75  LYS   A O   1 
ATOM   605  C CB  . LYS   A 1 76 ? 4.518   -32.000 1.499   1.00 52.27  ? 75  LYS   A CB  1 
ATOM   606  C CG  . LYS   A 1 76 ? 5.698   -32.571 0.729   1.00 62.12  ? 75  LYS   A CG  1 
ATOM   607  C CD  . LYS   A 1 76 ? 5.238   -33.654 -0.247  1.00 58.83  ? 75  LYS   A CD  1 
ATOM   608  C CE  . LYS   A 1 76 ? 6.300   -34.030 -1.230  1.00 62.43  ? 75  LYS   A CE  1 
ATOM   609  N N   . GLY   A 1 77 ? 6.393   -29.268 2.755   1.00 47.64  ? 76  GLY   A N   1 
ATOM   610  C CA  . GLY   A 1 77 ? 7.157   -28.141 2.249   1.00 45.74  ? 76  GLY   A CA  1 
ATOM   611  C C   . GLY   A 1 77 ? 6.892   -26.878 3.060   1.00 47.28  ? 76  GLY   A C   1 
ATOM   612  O O   . GLY   A 1 77 ? 7.629   -25.900 2.953   1.00 44.46  ? 76  GLY   A O   1 
ATOM   613  N N   . PHE   A 1 78 ? 5.882   -26.951 3.927   1.00 44.54  ? 77  PHE   A N   1 
ATOM   614  C CA  . PHE   A 1 78 ? 5.352   -25.750 4.534   1.00 46.56  ? 77  PHE   A CA  1 
ATOM   615  C C   . PHE   A 1 78 ? 6.330   -25.181 5.559   1.00 48.65  ? 77  PHE   A C   1 
ATOM   616  O O   . PHE   A 1 78 ? 6.515   -23.954 5.643   1.00 45.99  ? 77  PHE   A O   1 
ATOM   617  C CB  . PHE   A 1 78 ? 3.973   -26.031 5.132   1.00 40.71  ? 77  PHE   A CB  1 
ATOM   618  C CG  . PHE   A 1 78 ? 3.285   -24.785 5.663   1.00 40.02  ? 77  PHE   A CG  1 
ATOM   619  C CD1 . PHE   A 1 78 ? 3.466   -24.377 6.978   1.00 38.44  ? 77  PHE   A CD1 1 
ATOM   620  C CD2 . PHE   A 1 78 ? 2.445   -24.036 4.836   1.00 38.18  ? 77  PHE   A CD2 1 
ATOM   621  C CE1 . PHE   A 1 78 ? 2.839   -23.228 7.442   1.00 36.57  ? 77  PHE   A CE1 1 
ATOM   622  C CE2 . PHE   A 1 78 ? 1.803   -22.906 5.319   1.00 36.50  ? 77  PHE   A CE2 1 
ATOM   623  C CZ  . PHE   A 1 78 ? 2.004   -22.505 6.620   1.00 36.19  ? 77  PHE   A CZ  1 
ATOM   624  N N   . ASN   A 1 79 ? 6.904   -26.059 6.381   1.00 39.43  ? 78  ASN   A N   1 
ATOM   625  C CA  . ASN   A 1 79 ? 7.735   -25.545 7.463   1.00 43.08  ? 78  ASN   A CA  1 
ATOM   626  C C   . ASN   A 1 79 ? 9.073   -25.038 6.919   1.00 43.80  ? 78  ASN   A C   1 
ATOM   627  O O   . ASN   A 1 79 ? 9.635   -24.050 7.414   1.00 40.41  ? 78  ASN   A O   1 
ATOM   628  C CB  . ASN   A 1 79 ? 7.846   -26.537 8.609   1.00 41.54  ? 78  ASN   A CB  1 
ATOM   629  C CG  . ASN   A 1 79 ? 6.506   -26.756 9.260   1.00 45.71  ? 78  ASN   A CG  1 
ATOM   630  O OD1 . ASN   A 1 79 ? 5.755   -25.802 9.457   1.00 43.61  ? 78  ASN   A OD1 1 
ATOM   631  N ND2 . ASN   A 1 79 ? 6.162   -28.005 9.546   1.00 52.05  ? 78  ASN   A ND2 1 
ATOM   632  N N   . GLU   A 1 80 ? 9.543   -25.714 5.862   1.00 41.34  ? 79  GLU   A N   1 
ATOM   633  C CA  . GLU   A 1 80 ? 10.683  -25.237 5.112   1.00 41.79  ? 79  GLU   A CA  1 
ATOM   634  C C   . GLU   A 1 80 ? 10.336  -23.848 4.586   1.00 38.37  ? 79  GLU   A C   1 
ATOM   635  O O   . GLU   A 1 80 ? 11.142  -22.909 4.677   1.00 36.93  ? 79  GLU   A O   1 
ATOM   636  C CB  . GLU   A 1 80 ? 11.002  -26.222 3.990   1.00 42.55  ? 79  GLU   A CB  1 
ATOM   637  C CG  . GLU   A 1 80 ? 12.406  -26.036 3.431   1.00 47.73  ? 79  GLU   A CG  1 
ATOM   638  C CD  . GLU   A 1 80 ? 12.821  -27.056 2.385   1.00 59.84  ? 79  GLU   A CD  1 
ATOM   639  O OE1 . GLU   A 1 80 ? 12.562  -28.263 2.584   1.00 58.02  ? 79  GLU   A OE1 1 
ATOM   640  O OE2 . GLU   A 1 80 ? 13.424  -26.644 1.373   1.00 64.88  ? 79  GLU   A OE2 1 
ATOM   641  N N   . GLY   A 1 81 ? 9.121   -23.764 4.026   1.00 38.88  ? 80  GLY   A N   1 
ATOM   642  C CA  . GLY   A 1 81 ? 8.556   -22.536 3.488   1.00 37.14  ? 80  GLY   A CA  1 
ATOM   643  C C   . GLY   A 1 81 ? 8.644   -21.414 4.513   1.00 33.86  ? 80  GLY   A C   1 
ATOM   644  O O   . GLY   A 1 81 ? 9.069   -20.316 4.178   1.00 31.08  ? 80  GLY   A O   1 
ATOM   645  N N   . LEU   A 1 82 ? 8.280   -21.727 5.765   1.00 31.01  ? 81  LEU   A N   1 
ATOM   646  C CA  . LEU   A 1 82 ? 8.220   -20.730 6.827   1.00 31.55  ? 81  LEU   A CA  1 
ATOM   647  C C   . LEU   A 1 82 ? 9.607   -20.164 7.091   1.00 28.22  ? 81  LEU   A C   1 
ATOM   648  O O   . LEU   A 1 82 ? 9.761   -18.955 7.309   1.00 30.87  ? 81  LEU   A O   1 
ATOM   649  C CB  . LEU   A 1 82 ? 7.563   -21.178 8.144   1.00 34.53  ? 81  LEU   A CB  1 
ATOM   650  C CG  . LEU   A 1 82 ? 6.025   -21.228 8.201   1.00 37.14  ? 81  LEU   A CG  1 
ATOM   651  C CD1 . LEU   A 1 82 ? 5.577   -21.062 9.653   1.00 40.39  ? 81  LEU   A CD1 1 
ATOM   652  C CD2 . LEU   A 1 82 ? 5.268   -20.217 7.361   1.00 35.30  ? 81  LEU   A CD2 1 
ATOM   653  N N   . TRP   A 1 83 ? 10.593  -21.071 7.153   1.00 35.23  ? 82  TRP   A N   1 
ATOM   654  C CA  . TRP   A 1 83 ? 11.987  -20.731 7.394   1.00 31.26  ? 82  TRP   A CA  1 
ATOM   655  C C   . TRP   A 1 83 ? 12.507  -19.854 6.261   1.00 35.01  ? 82  TRP   A C   1 
ATOM   656  O O   . TRP   A 1 83 ? 13.179  -18.852 6.516   1.00 36.29  ? 82  TRP   A O   1 
ATOM   657  C CB  . TRP   A 1 83 ? 12.828  -22.008 7.499   1.00 35.82  ? 82  TRP   A CB  1 
ATOM   658  C CG  . TRP   A 1 83 ? 14.268  -21.694 7.786   1.00 33.93  ? 82  TRP   A CG  1 
ATOM   659  C CD1 . TRP   A 1 83 ? 14.865  -21.576 9.011   1.00 28.01  ? 82  TRP   A CD1 1 
ATOM   660  C CD2 . TRP   A 1 83 ? 15.261  -21.365 6.794   1.00 29.39  ? 82  TRP   A CD2 1 
ATOM   661  N NE1 . TRP   A 1 83 ? 16.176  -21.252 8.839   1.00 33.41  ? 82  TRP   A NE1 1 
ATOM   662  C CE2 . TRP   A 1 83 ? 16.447  -21.096 7.501   1.00 31.89  ? 82  TRP   A CE2 1 
ATOM   663  C CE3 . TRP   A 1 83 ? 15.249  -21.279 5.395   1.00 31.06  ? 82  TRP   A CE3 1 
ATOM   664  C CZ2 . TRP   A 1 83 ? 17.627  -20.735 6.851   1.00 38.01  ? 82  TRP   A CZ2 1 
ATOM   665  C CZ3 . TRP   A 1 83 ? 16.405  -20.902 4.747   1.00 36.33  ? 82  TRP   A CZ3 1 
ATOM   666  C CH2 . TRP   A 1 83 ? 17.576  -20.627 5.476   1.00 41.88  ? 82  TRP   A CH2 1 
ATOM   667  N N   . GLU   A 1 84 ? 12.177  -20.212 5.008   1.00 31.66  ? 83  GLU   A N   1 
ATOM   668  C CA  . GLU   A 1 84 ? 12.715  -19.441 3.894   1.00 33.20  ? 83  GLU   A CA  1 
ATOM   669  C C   . GLU   A 1 84 ? 12.207  -17.993 3.929   1.00 38.20  ? 83  GLU   A C   1 
ATOM   670  O O   . GLU   A 1 84 ? 12.949  -17.035 3.690   1.00 39.20  ? 83  GLU   A O   1 
ATOM   671  C CB  . GLU   A 1 84 ? 12.377  -20.104 2.563   1.00 29.06  ? 83  GLU   A CB  1 
ATOM   672  C CG  . GLU   A 1 84 ? 12.970  -21.497 2.394   1.00 34.58  ? 83  GLU   A CG  1 
ATOM   673  C CD  . GLU   A 1 84 ? 12.564  -22.162 1.072   1.00 37.54  ? 83  GLU   A CD  1 
ATOM   674  O OE1 . GLU   A 1 84 ? 11.626  -21.652 0.441   1.00 34.73  ? 83  GLU   A OE1 1 
ATOM   675  O OE2 . GLU   A 1 84 ? 13.156  -23.186 0.670   1.00 33.56  ? 83  GLU   A OE2 1 
ATOM   676  N N   . ILE   A 1 85 ? 10.917  -17.816 4.208   1.00 36.40  ? 84  ILE   A N   1 
ATOM   677  C CA  . ILE   A 1 85 ? 10.337  -16.490 4.064   1.00 38.12  ? 84  ILE   A CA  1 
ATOM   678  C C   . ILE   A 1 85 ? 10.893  -15.607 5.186   1.00 38.26  ? 84  ILE   A C   1 
ATOM   679  O O   . ILE   A 1 85 ? 11.005  -14.397 5.018   1.00 43.03  ? 84  ILE   A O   1 
ATOM   680  C CB  . ILE   A 1 85 ? 8.786   -16.552 4.022   1.00 35.40  ? 84  ILE   A CB  1 
ATOM   681  C CG1 . ILE   A 1 85 ? 8.140   -15.156 3.728   1.00 34.33  ? 84  ILE   A CG1 1 
ATOM   682  C CG2 . ILE   A 1 85 ? 8.228   -17.196 5.301   1.00 27.44  ? 84  ILE   A CG2 1 
ATOM   683  C CD1 . ILE   A 1 85 ? 6.800   -15.178 3.003   1.00 30.13  ? 84  ILE   A CD1 1 
ATOM   684  N N   . GLN   A 1 86 ? 11.277  -16.229 6.311   1.00 33.96  ? 85  GLN   A N   1 
ATOM   685  C CA  . GLN   A 1 86 ? 11.702  -15.495 7.493   1.00 33.49  ? 85  GLN   A CA  1 
ATOM   686  C C   . GLN   A 1 86 ? 13.188  -15.182 7.395   1.00 33.37  ? 85  GLN   A C   1 
ATOM   687  O O   . GLN   A 1 86 ? 13.609  -14.091 7.750   1.00 42.48  ? 85  GLN   A O   1 
ATOM   688  C CB  . GLN   A 1 86 ? 11.380  -16.182 8.816   1.00 28.57  ? 85  GLN   A CB  1 
ATOM   689  C CG  . GLN   A 1 86 ? 11.889  -15.434 10.047  1.00 35.25  ? 85  GLN   A CG  1 
ATOM   690  C CD  . GLN   A 1 86 ? 11.274  -15.949 11.337  1.00 46.06  ? 85  GLN   A CD  1 
ATOM   691  O OE1 . GLN   A 1 86 ? 10.756  -17.076 11.397  1.00 50.20  ? 85  GLN   A OE1 1 
ATOM   692  N NE2 . GLN   A 1 86 ? 11.328  -15.143 12.395  1.00 43.77  ? 85  GLN   A NE2 1 
ATOM   693  N N   . ASN   A 1 87 ? 13.950  -16.115 6.834   1.00 33.01  ? 86  ASN   A N   1 
ATOM   694  C CA  . ASN   A 1 87 ? 15.401  -16.151 6.945   1.00 26.72  ? 86  ASN   A CA  1 
ATOM   695  C C   . ASN   A 1 87 ? 16.080  -15.829 5.613   1.00 27.83  ? 86  ASN   A C   1 
ATOM   696  O O   . ASN   A 1 87 ? 17.213  -15.349 5.639   1.00 32.90  ? 86  ASN   A O   1 
ATOM   697  C CB  . ASN   A 1 87 ? 15.855  -17.475 7.556   1.00 30.19  ? 86  ASN   A CB  1 
ATOM   698  C CG  . ASN   A 1 87 ? 15.263  -17.629 8.944   1.00 35.59  ? 86  ASN   A CG  1 
ATOM   699  O OD1 . ASN   A 1 87 ? 15.741  -16.977 9.877   1.00 31.47  ? 86  ASN   A OD1 1 
ATOM   700  N ND2 . ASN   A 1 87 ? 14.202  -18.421 9.101   1.00 29.25  ? 86  ASN   A ND2 1 
ATOM   701  N N   . ASN   A 1 88 ? 15.435  -16.048 4.449   1.00 26.25  ? 87  ASN   A N   1 
ATOM   702  C CA  . ASN   A 1 88 ? 16.139  -15.715 3.208   1.00 24.64  ? 87  ASN   A CA  1 
ATOM   703  C C   . ASN   A 1 88 ? 15.184  -15.641 2.034   1.00 27.61  ? 87  ASN   A C   1 
ATOM   704  O O   . ASN   A 1 88 ? 15.425  -16.276 1.003   1.00 27.41  ? 87  ASN   A O   1 
ATOM   705  C CB  . ASN   A 1 88 ? 17.365  -16.579 2.932   1.00 35.97  ? 87  ASN   A CB  1 
ATOM   706  C CG  . ASN   A 1 88 ? 18.256  -16.023 1.844   1.00 38.31  ? 87  ASN   A CG  1 
ATOM   707  O OD1 . ASN   A 1 88 ? 17.846  -15.158 1.063   1.00 39.57  ? 87  ASN   A OD1 1 
ATOM   708  N ND2 . ASN   A 1 88 ? 19.477  -16.526 1.761   1.00 41.46  ? 87  ASN   A ND2 1 
ATOM   709  N N   . PRO   A 1 89 ? 14.177  -14.729 2.102   1.00 31.54  ? 88  PRO   A N   1 
ATOM   710  C CA  . PRO   A 1 89 ? 13.045  -14.761 1.176   1.00 33.55  ? 88  PRO   A CA  1 
ATOM   711  C C   . PRO   A 1 89 ? 13.423  -14.408 -0.262  1.00 35.14  ? 88  PRO   A C   1 
ATOM   712  O O   . PRO   A 1 89 ? 12.676  -14.685 -1.200  1.00 46.08  ? 88  PRO   A O   1 
ATOM   713  C CB  . PRO   A 1 89 ? 12.036  -13.794 1.777   1.00 33.64  ? 88  PRO   A CB  1 
ATOM   714  C CG  . PRO   A 1 89 ? 12.862  -12.865 2.666   1.00 34.86  ? 88  PRO   A CG  1 
ATOM   715  C CD  . PRO   A 1 89 ? 14.102  -13.625 3.062   1.00 29.23  ? 88  PRO   A CD  1 
ATOM   716  N N   . HIS   A 1 90 ? 14.610  -13.847 -0.434  1.00 35.10  ? 89  HIS   A N   1 
ATOM   717  C CA  . HIS   A 1 90 ? 15.003  -13.320 -1.724  1.00 35.03  ? 89  HIS   A CA  1 
ATOM   718  C C   . HIS   A 1 90 ? 16.135  -14.124 -2.358  1.00 39.14  ? 89  HIS   A C   1 
ATOM   719  O O   . HIS   A 1 90 ? 16.676  -13.676 -3.360  1.00 40.29  ? 89  HIS   A O   1 
ATOM   720  C CB  . HIS   A 1 90 ? 15.424  -11.861 -1.560  1.00 34.03  ? 89  HIS   A CB  1 
ATOM   721  C CG  . HIS   A 1 90 ? 14.343  -11.040 -0.957  1.00 39.43  ? 89  HIS   A CG  1 
ATOM   722  N ND1 . HIS   A 1 90 ? 13.093  -10.917 -1.528  1.00 32.65  ? 89  HIS   A ND1 1 
ATOM   723  C CD2 . HIS   A 1 90 ? 14.330  -10.279 0.166   1.00 40.05  ? 89  HIS   A CD2 1 
ATOM   724  C CE1 . HIS   A 1 90 ? 12.356  -10.113 -0.774  1.00 38.80  ? 89  HIS   A CE1 1 
ATOM   725  N NE2 . HIS   A 1 90 ? 13.078  -9.710  0.260   1.00 42.40  ? 89  HIS   A NE2 1 
ATOM   726  N N   . ALA   A 1 91 ? 16.453  -15.320 -1.827  1.00 38.90  ? 90  ALA   A N   1 
ATOM   727  C CA  . ALA   A 1 91 ? 17.483  -16.159 -2.424  1.00 38.29  ? 90  ALA   A CA  1 
ATOM   728  C C   . ALA   A 1 91 ? 17.004  -16.767 -3.743  1.00 38.62  ? 90  ALA   A C   1 
ATOM   729  O O   . ALA   A 1 91 ? 15.810  -16.799 -4.030  1.00 38.67  ? 90  ALA   A O   1 
ATOM   730  C CB  . ALA   A 1 91 ? 17.867  -17.263 -1.461  1.00 34.87  ? 90  ALA   A CB  1 
ATOM   731  N N   . SER   A 1 92 ? 17.955  -17.260 -4.539  1.00 39.92  ? 91  SER   A N   1 
ATOM   732  C CA  . SER   A 1 92 ? 17.649  -18.157 -5.641  1.00 43.72  ? 91  SER   A CA  1 
ATOM   733  C C   . SER   A 1 92 ? 17.481  -19.580 -5.108  1.00 44.50  ? 91  SER   A C   1 
ATOM   734  O O   . SER   A 1 92 ? 18.420  -20.154 -4.546  1.00 54.36  ? 91  SER   A O   1 
ATOM   735  C CB  . SER   A 1 92 ? 18.713  -18.108 -6.688  1.00 48.97  ? 91  SER   A CB  1 
ATOM   736  O OG  . SER   A 1 92 ? 18.841  -19.388 -7.291  1.00 56.22  ? 91  SER   A OG  1 
ATOM   737  N N   . TYR   A 1 93 ? 16.259  -20.115 -5.236  1.00 40.15  ? 92  TYR   A N   1 
ATOM   738  C CA  . TYR   A 1 93 ? 15.990  -21.489 -4.851  1.00 41.34  ? 92  TYR   A CA  1 
ATOM   739  C C   . TYR   A 1 93 ? 15.845  -22.349 -6.105  1.00 48.17  ? 92  TYR   A C   1 
ATOM   740  O O   . TYR   A 1 93 ? 15.315  -23.458 -6.038  1.00 49.65  ? 92  TYR   A O   1 
ATOM   741  C CB  . TYR   A 1 93 ? 14.753  -21.574 -3.959  1.00 39.77  ? 92  TYR   A CB  1 
ATOM   742  C CG  . TYR   A 1 93 ? 14.864  -20.911 -2.595  1.00 36.68  ? 92  TYR   A CG  1 
ATOM   743  C CD1 . TYR   A 1 93 ? 15.331  -21.613 -1.490  1.00 36.77  ? 92  TYR   A CD1 1 
ATOM   744  C CD2 . TYR   A 1 93 ? 14.447  -19.606 -2.397  1.00 31.21  ? 92  TYR   A CD2 1 
ATOM   745  C CE1 . TYR   A 1 93 ? 15.409  -21.020 -0.237  1.00 37.09  ? 92  TYR   A CE1 1 
ATOM   746  C CE2 . TYR   A 1 93 ? 14.522  -19.010 -1.153  1.00 29.75  ? 92  TYR   A CE2 1 
ATOM   747  C CZ  . TYR   A 1 93 ? 14.999  -19.714 -0.060  1.00 33.51  ? 92  TYR   A CZ  1 
ATOM   748  O OH  . TYR   A 1 93 ? 15.099  -19.123 1.175   1.00 30.11  ? 92  TYR   A OH  1 
ATOM   749  N N   . SER   A 1 94 ? 16.363  -21.844 -7.234  1.00 53.30  ? 93  SER   A N   1 
ATOM   750  C CA  . SER   A 1 94 ? 16.347  -22.541 -8.512  1.00 66.43  ? 93  SER   A CA  1 
ATOM   751  C C   . SER   A 1 94 ? 16.663  -24.031 -8.315  1.00 75.92  ? 93  SER   A C   1 
ATOM   752  O O   . SER   A 1 94 ? 17.597  -24.347 -7.524  1.00 74.28  ? 93  SER   A O   1 
ATOM   753  C CB  . SER   A 1 94 ? 17.297  -21.921 -9.511  1.00 62.47  ? 93  SER   A CB  1 
ATOM   754  O OG  . SER   A 1 94 ? 17.065  -20.527 -9.661  1.00 72.12  ? 93  SER   A OG  1 
ATOM   755  O OXT . SER   A 1 94 ? 15.965  -24.827 -8.969  1.00 104.61 ? 93  SER   A OXT 1 
ATOM   756  N N   . MET   B 1 2  ? 39.052  -11.254 -41.487 1.00 95.08  ? 1   MET   B N   1 
ATOM   757  C CA  . MET   B 1 2  ? 38.705  -12.179 -42.599 1.00 94.97  ? 1   MET   B CA  1 
ATOM   758  C C   . MET   B 1 2  ? 37.182  -12.241 -42.724 1.00 90.56  ? 1   MET   B C   1 
ATOM   759  O O   . MET   B 1 2  ? 36.490  -12.389 -41.716 1.00 86.56  ? 1   MET   B O   1 
ATOM   760  C CB  . MET   B 1 2  ? 39.292  -13.576 -42.340 1.00 96.09  ? 1   MET   B CB  1 
ATOM   761  C CG  . MET   B 1 2  ? 39.410  -14.476 -43.573 1.00 98.91  ? 1   MET   B CG  1 
ATOM   762  S SD  . MET   B 1 2  ? 40.477  -13.925 -44.926 1.00 88.38  ? 1   MET   B SD  1 
ATOM   763  C CE  . MET   B 1 2  ? 41.972  -13.493 -44.026 1.00 80.62  ? 1   MET   B CE  1 
ATOM   764  N N   . PRO   B 1 3  ? 36.612  -12.078 -43.945 1.00 86.95  ? 2   PRO   B N   1 
ATOM   765  C CA  . PRO   B 1 3  ? 35.200  -12.389 -44.190 1.00 82.84  ? 2   PRO   B CA  1 
ATOM   766  C C   . PRO   B 1 3  ? 34.794  -13.811 -43.808 1.00 82.79  ? 2   PRO   B C   1 
ATOM   767  O O   . PRO   B 1 3  ? 35.433  -14.786 -44.209 1.00 77.65  ? 2   PRO   B O   1 
ATOM   768  C CB  . PRO   B 1 3  ? 35.026  -12.118 -45.693 1.00 75.38  ? 2   PRO   B CB  1 
ATOM   769  C CG  . PRO   B 1 3  ? 36.084  -11.088 -45.986 1.00 70.16  ? 2   PRO   B CG  1 
ATOM   770  C CD  . PRO   B 1 3  ? 37.273  -11.520 -45.139 1.00 77.68  ? 2   PRO   B CD  1 
ATOM   771  N N   . HIS   B 1 4  ? 33.722  -13.890 -43.013 1.00 79.61  ? 3   HIS   B N   1 
ATOM   772  C CA  . HIS   B 1 4  ? 33.126  -15.150 -42.601 1.00 84.41  ? 3   HIS   B CA  1 
ATOM   773  C C   . HIS   B 1 4  ? 31.734  -15.279 -43.222 1.00 85.39  ? 3   HIS   B C   1 
ATOM   774  O O   . HIS   B 1 4  ? 31.223  -14.321 -43.807 1.00 89.06  ? 3   HIS   B O   1 
ATOM   775  C CB  . HIS   B 1 4  ? 33.131  -15.264 -41.073 1.00 79.67  ? 3   HIS   B CB  1 
ATOM   776  C CG  . HIS   B 1 4  ? 34.488  -15.413 -40.459 1.00 79.50  ? 3   HIS   B CG  1 
ATOM   777  N ND1 . HIS   B 1 4  ? 35.580  -15.942 -41.116 1.00 80.96  ? 3   HIS   B ND1 1 
ATOM   778  C CD2 . HIS   B 1 4  ? 34.910  -15.112 -39.218 1.00 73.77  ? 3   HIS   B CD2 1 
ATOM   779  C CE1 . HIS   B 1 4  ? 36.621  -15.945 -40.294 1.00 73.74  ? 3   HIS   B CE1 1 
ATOM   780  N NE2 . HIS   B 1 4  ? 36.233  -15.447 -39.137 1.00 70.70  ? 3   HIS   B NE2 1 
ATOM   781  N N   . ALA   B 1 5  ? 31.131  -16.473 -43.104 1.00 75.70  ? 4   ALA   B N   1 
ATOM   782  C CA  . ALA   B 1 5  ? 29.842  -16.750 -43.721 1.00 59.70  ? 4   ALA   B CA  1 
ATOM   783  C C   . ALA   B 1 5  ? 28.776  -15.901 -43.040 1.00 53.34  ? 4   ALA   B C   1 
ATOM   784  O O   . ALA   B 1 5  ? 27.933  -15.306 -43.713 1.00 50.71  ? 4   ALA   B O   1 
ATOM   785  C CB  . ALA   B 1 5  ? 29.537  -18.222 -43.647 1.00 60.81  ? 4   ALA   B CB  1 
ATOM   786  N N   . PHE   B 1 6  ? 28.844  -15.844 -41.704 1.00 47.07  ? 5   PHE   B N   1 
ATOM   787  C CA  . PHE   B 1 6  ? 28.092  -14.859 -40.943 1.00 57.02  ? 5   PHE   B CA  1 
ATOM   788  C C   . PHE   B 1 6  ? 28.941  -13.587 -40.783 1.00 66.86  ? 5   PHE   B C   1 
ATOM   789  O O   . PHE   B 1 6  ? 30.092  -13.649 -40.347 1.00 71.60  ? 5   PHE   B O   1 
ATOM   790  C CB  . PHE   B 1 6  ? 27.532  -15.445 -39.636 1.00 48.31  ? 5   PHE   B CB  1 
ATOM   791  C CG  . PHE   B 1 6  ? 26.366  -16.411 -39.816 1.00 47.16  ? 5   PHE   B CG  1 
ATOM   792  C CD1 . PHE   B 1 6  ? 25.066  -15.939 -39.961 1.00 42.57  ? 5   PHE   B CD1 1 
ATOM   793  C CD2 . PHE   B 1 6  ? 26.569  -17.796 -39.855 1.00 46.59  ? 5   PHE   B CD2 1 
ATOM   794  C CE1 . PHE   B 1 6  ? 24.006  -16.817 -40.160 1.00 47.34  ? 5   PHE   B CE1 1 
ATOM   795  C CE2 . PHE   B 1 6  ? 25.506  -18.670 -40.061 1.00 48.33  ? 5   PHE   B CE2 1 
ATOM   796  C CZ  . PHE   B 1 6  ? 24.223  -18.183 -40.187 1.00 47.05  ? 5   PHE   B CZ  1 
ATOM   797  N N   . LYS   B 1 7  ? 28.362  -12.431 -41.150 1.00 63.88  ? 6   LYS   B N   1 
ATOM   798  C CA  . LYS   B 1 7  ? 29.000  -11.127 -41.038 1.00 63.61  ? 6   LYS   B CA  1 
ATOM   799  C C   . LYS   B 1 7  ? 28.250  -10.285 -40.003 1.00 67.46  ? 6   LYS   B C   1 
ATOM   800  O O   . LYS   B 1 7  ? 27.020  -10.345 -39.917 1.00 56.18  ? 6   LYS   B O   1 
ATOM   801  C CB  . LYS   B 1 7  ? 29.003  -10.439 -42.410 1.00 66.56  ? 6   LYS   B CB  1 
ATOM   802  C CG  . LYS   B 1 7  ? 27.627  -10.298 -43.046 1.00 68.00  ? 6   LYS   B CG  1 
ATOM   803  C CD  . LYS   B 1 7  ? 27.629  -10.009 -44.540 1.00 73.24  ? 6   LYS   B CD  1 
ATOM   804  C CE  . LYS   B 1 7  ? 26.416  -10.594 -45.197 1.00 72.39  ? 6   LYS   B CE  1 
ATOM   805  N NZ  . LYS   B 1 7  ? 26.411  -12.061 -45.136 1.00 64.48  ? 6   LYS   B NZ  1 
ATOM   806  N N   . PRO   B 1 8  ? 28.949  -9.428  -39.219 1.00 64.31  ? 7   PRO   B N   1 
ATOM   807  C CA  . PRO   B 1 8  ? 28.339  -8.807  -38.050 1.00 62.97  ? 7   PRO   B CA  1 
ATOM   808  C C   . PRO   B 1 8  ? 27.334  -7.780  -38.558 1.00 68.62  ? 7   PRO   B C   1 
ATOM   809  O O   . PRO   B 1 8  ? 27.700  -6.841  -39.265 1.00 69.48  ? 7   PRO   B O   1 
ATOM   810  C CB  . PRO   B 1 8  ? 29.521  -8.188  -37.304 1.00 60.28  ? 7   PRO   B CB  1 
ATOM   811  C CG  . PRO   B 1 8  ? 30.724  -8.785  -37.973 1.00 55.31  ? 7   PRO   B CG  1 
ATOM   812  C CD  . PRO   B 1 8  ? 30.321  -8.954  -39.435 1.00 59.56  ? 7   PRO   B CD  1 
ATOM   813  N N   . GLY   B 1 9  ? 26.063  -8.011  -38.202 1.00 58.51  ? 8   GLY   B N   1 
ATOM   814  C CA  . GLY   B 1 9  ? 24.954  -7.210  -38.668 1.00 50.36  ? 8   GLY   B CA  1 
ATOM   815  C C   . GLY   B 1 9  ? 23.945  -8.101  -39.372 1.00 45.26  ? 8   GLY   B C   1 
ATOM   816  O O   . GLY   B 1 9  ? 22.823  -7.673  -39.640 1.00 49.57  ? 8   GLY   B O   1 
ATOM   817  N N   . ASP   B 1 10 ? 24.371  -9.339  -39.657 1.00 49.13  ? 9   ASP   B N   1 
ATOM   818  C CA  . ASP   B 1 10 ? 23.499  -10.409 -40.142 1.00 44.61  ? 9   ASP   B CA  1 
ATOM   819  C C   . ASP   B 1 10 ? 22.353  -10.675 -39.161 1.00 46.66  ? 9   ASP   B C   1 
ATOM   820  O O   . ASP   B 1 10 ? 22.561  -10.827 -37.950 1.00 46.35  ? 9   ASP   B O   1 
ATOM   821  C CB  . ASP   B 1 10 ? 24.278  -11.683 -40.430 1.00 55.88  ? 9   ASP   B CB  1 
ATOM   822  C CG  . ASP   B 1 10 ? 24.818  -11.834 -41.845 1.00 62.17  ? 9   ASP   B CG  1 
ATOM   823  O OD1 . ASP   B 1 10 ? 24.303  -11.134 -42.761 1.00 62.05  ? 9   ASP   B OD1 1 
ATOM   824  O OD2 . ASP   B 1 10 ? 25.751  -12.644 -42.016 1.00 53.06  ? 9   ASP   B OD2 1 
ATOM   825  N N   . LEU   B 1 11 ? 21.137  -10.736 -39.703 1.00 35.63  ? 10  LEU   B N   1 
ATOM   826  C CA  . LEU   B 1 11 ? 19.960  -10.922 -38.886 1.00 37.85  ? 10  LEU   B CA  1 
ATOM   827  C C   . LEU   B 1 11 ? 19.601  -12.398 -38.854 1.00 39.98  ? 10  LEU   B C   1 
ATOM   828  O O   . LEU   B 1 11 ? 19.496  -13.010 -39.918 1.00 36.02  ? 10  LEU   B O   1 
ATOM   829  C CB  . LEU   B 1 11 ? 18.864  -10.098 -39.549 1.00 38.03  ? 10  LEU   B CB  1 
ATOM   830  C CG  . LEU   B 1 11 ? 19.140  -8.595  -39.607 1.00 33.00  ? 10  LEU   B CG  1 
ATOM   831  C CD1 . LEU   B 1 11 ? 17.849  -7.897  -39.925 1.00 31.22  ? 10  LEU   B CD1 1 
ATOM   832  C CD2 . LEU   B 1 11 ? 19.651  -8.173  -38.235 1.00 36.71  ? 10  LEU   B CD2 1 
ATOM   833  N N   . VAL   B 1 12 ? 19.423  -12.953 -37.640 1.00 37.64  ? 11  VAL   B N   1 
ATOM   834  C CA  . VAL   B 1 12 ? 19.062  -14.361 -37.544 1.00 43.41  ? 11  VAL   B CA  1 
ATOM   835  C C   . VAL   B 1 12 ? 17.928  -14.555 -36.546 1.00 48.18  ? 11  VAL   B C   1 
ATOM   836  O O   . VAL   B 1 12 ? 17.538  -13.620 -35.835 1.00 43.04  ? 11  VAL   B O   1 
ATOM   837  C CB  . VAL   B 1 12 ? 20.181  -15.387 -37.247 1.00 42.61  ? 11  VAL   B CB  1 
ATOM   838  C CG1 . VAL   B 1 12 ? 21.198  -15.494 -38.387 1.00 40.44  ? 11  VAL   B CG1 1 
ATOM   839  C CG2 . VAL   B 1 12 ? 20.850  -15.172 -35.886 1.00 40.27  ? 11  VAL   B CG2 1 
ATOM   840  N N   . PHE   B 1 13 ? 17.420  -15.797 -36.549 1.00 39.93  ? 12  PHE   B N   1 
ATOM   841  C CA  . PHE   B 1 13 ? 16.887  -16.416 -35.360 1.00 40.81  ? 12  PHE   B CA  1 
ATOM   842  C C   . PHE   B 1 13 ? 18.000  -17.284 -34.789 1.00 45.04  ? 12  PHE   B C   1 
ATOM   843  O O   . PHE   B 1 13 ? 18.659  -17.979 -35.567 1.00 41.38  ? 12  PHE   B O   1 
ATOM   844  C CB  . PHE   B 1 13 ? 15.682  -17.269 -35.746 1.00 39.49  ? 12  PHE   B CB  1 
ATOM   845  C CG  . PHE   B 1 13 ? 14.482  -16.411 -36.091 1.00 42.24  ? 12  PHE   B CG  1 
ATOM   846  C CD1 . PHE   B 1 13 ? 14.189  -16.106 -37.413 1.00 41.61  ? 12  PHE   B CD1 1 
ATOM   847  C CD2 . PHE   B 1 13 ? 13.671  -15.884 -35.088 1.00 43.01  ? 12  PHE   B CD2 1 
ATOM   848  C CE1 . PHE   B 1 13 ? 13.082  -15.332 -37.729 1.00 44.71  ? 12  PHE   B CE1 1 
ATOM   849  C CE2 . PHE   B 1 13 ? 12.567  -15.105 -35.406 1.00 39.97  ? 12  PHE   B CE2 1 
ATOM   850  C CZ  . PHE   B 1 13 ? 12.282  -14.826 -36.723 1.00 46.73  ? 12  PHE   B CZ  1 
ATOM   851  N N   . ALA   B 1 14 ? 18.192  -17.183 -33.455 1.00 41.07  ? 13  ALA   B N   1 
ATOM   852  C CA  . ALA   B 1 14 ? 19.174  -17.919 -32.669 1.00 38.72  ? 13  ALA   B CA  1 
ATOM   853  C C   . ALA   B 1 14 ? 18.489  -18.892 -31.700 1.00 42.05  ? 13  ALA   B C   1 
ATOM   854  O O   . ALA   B 1 14 ? 17.510  -18.542 -31.033 1.00 38.47  ? 13  ALA   B O   1 
ATOM   855  C CB  . ALA   B 1 14 ? 20.057  -16.929 -31.944 1.00 44.17  ? 13  ALA   B CB  1 
ATOM   856  N N   . LYS   B 1 15 ? 19.003  -20.130 -31.627 1.00 42.40  ? 14  LYS   B N   1 
ATOM   857  C CA  . LYS   B 1 15 ? 18.363  -21.185 -30.857 1.00 42.40  ? 14  LYS   B CA  1 
ATOM   858  C C   . LYS   B 1 15 ? 19.147  -21.414 -29.574 1.00 43.45  ? 14  LYS   B C   1 
ATOM   859  O O   . LYS   B 1 15 ? 20.364  -21.543 -29.614 1.00 48.33  ? 14  LYS   B O   1 
ATOM   860  C CB  . LYS   B 1 15 ? 18.284  -22.520 -31.615 1.00 42.96  ? 14  LYS   B CB  1 
ATOM   861  C CG  . LYS   B 1 15 ? 17.406  -23.614 -30.998 1.00 36.62  ? 14  LYS   B CG  1 
ATOM   862  C CD  . LYS   B 1 15 ? 15.965  -23.117 -30.842 1.00 46.01  ? 14  LYS   B CD  1 
ATOM   863  C CE  . LYS   B 1 15 ? 14.947  -24.007 -30.206 1.00 44.38  ? 14  LYS   B CE  1 
ATOM   864  N NZ  . LYS   B 1 15 ? 15.286  -24.224 -28.796 1.00 40.77  ? 14  LYS   B NZ  1 
ATOM   865  N N   . MET   B 1 16 ? 18.435  -21.503 -28.447 1.00 46.04  ? 15  MET   B N   1 
ATOM   866  C CA  . MET   B 1 16 ? 19.063  -21.838 -27.178 1.00 47.43  ? 15  MET   B CA  1 
ATOM   867  C C   . MET   B 1 16 ? 18.253  -22.951 -26.521 1.00 47.48  ? 15  MET   B C   1 
ATOM   868  O O   . MET   B 1 16 ? 17.063  -23.095 -26.783 1.00 45.73  ? 15  MET   B O   1 
ATOM   869  C CB  . MET   B 1 16 ? 19.122  -20.624 -26.246 1.00 49.14  ? 15  MET   B CB  1 
ATOM   870  C CG  . MET   B 1 16 ? 19.829  -19.408 -26.818 1.00 56.08  ? 15  MET   B CG  1 
ATOM   871  S SD  . MET   B 1 16 ? 21.588  -19.183 -26.471 1.00 60.48  ? 15  MET   B SD  1 
ATOM   872  C CE  . MET   B 1 16 ? 21.520  -19.034 -24.678 1.00 50.36  ? 15  MET   B CE  1 
ATOM   873  N N   . LYS   B 1 17 ? 18.903  -23.753 -25.677 1.00 47.84  ? 16  LYS   B N   1 
ATOM   874  C CA  . LYS   B 1 17 ? 18.158  -24.788 -24.981 1.00 52.58  ? 16  LYS   B CA  1 
ATOM   875  C C   . LYS   B 1 17 ? 17.120  -24.110 -24.080 1.00 49.48  ? 16  LYS   B C   1 
ATOM   876  O O   . LYS   B 1 17 ? 17.458  -23.212 -23.315 1.00 48.56  ? 16  LYS   B O   1 
ATOM   877  C CB  . LYS   B 1 17 ? 19.118  -25.798 -24.328 1.00 56.41  ? 16  LYS   B CB  1 
ATOM   878  C CG  . LYS   B 1 17 ? 18.615  -27.253 -24.279 1.00 60.54  ? 16  LYS   B CG  1 
ATOM   879  C CD  . LYS   B 1 17 ? 19.626  -28.273 -23.762 1.00 53.78  ? 16  LYS   B CD  1 
ATOM   880  N N   . GLY   B 1 18 ? 15.848  -24.510 -24.214 1.00 51.16  ? 17  GLY   B N   1 
ATOM   881  C CA  . GLY   B 1 18 ? 14.789  -24.068 -23.318 1.00 46.03  ? 17  GLY   B CA  1 
ATOM   882  C C   . GLY   B 1 18 ? 14.091  -22.789 -23.786 1.00 49.25  ? 17  GLY   B C   1 
ATOM   883  O O   . GLY   B 1 18 ? 13.400  -22.140 -22.995 1.00 43.93  ? 17  GLY   B O   1 
ATOM   884  N N   . TYR   B 1 19 ? 14.280  -22.434 -25.069 1.00 41.94  ? 18  TYR   B N   1 
ATOM   885  C CA  . TYR   B 1 19 ? 13.705  -21.235 -25.650 1.00 39.29  ? 18  TYR   B CA  1 
ATOM   886  C C   . TYR   B 1 19 ? 13.420  -21.513 -27.118 1.00 37.94  ? 18  TYR   B C   1 
ATOM   887  O O   . TYR   B 1 19 ? 14.032  -22.384 -27.731 1.00 38.25  ? 18  TYR   B O   1 
ATOM   888  C CB  . TYR   B 1 19 ? 14.571  -19.978 -25.474 1.00 45.42  ? 18  TYR   B CB  1 
ATOM   889  C CG  . TYR   B 1 19 ? 15.006  -19.846 -24.023 1.00 48.72  ? 18  TYR   B CG  1 
ATOM   890  C CD1 . TYR   B 1 19 ? 14.139  -19.336 -23.056 1.00 52.03  ? 18  TYR   B CD1 1 
ATOM   891  C CD2 . TYR   B 1 19 ? 16.248  -20.319 -23.606 1.00 47.51  ? 18  TYR   B CD2 1 
ATOM   892  C CE1 . TYR   B 1 19 ? 14.502  -19.301 -21.716 1.00 53.57  ? 18  TYR   B CE1 1 
ATOM   893  C CE2 . TYR   B 1 19 ? 16.624  -20.270 -22.270 1.00 49.03  ? 18  TYR   B CE2 1 
ATOM   894  C CZ  . TYR   B 1 19 ? 15.743  -19.774 -21.323 1.00 47.68  ? 18  TYR   B CZ  1 
ATOM   895  O OH  . TYR   B 1 19 ? 16.135  -19.727 -20.023 1.00 49.93  ? 18  TYR   B OH  1 
ATOM   896  N N   . PRO   B 1 20 ? 12.412  -20.847 -27.702 1.00 37.66  ? 19  PRO   B N   1 
ATOM   897  C CA  . PRO   B 1 20 ? 12.236  -20.887 -29.151 1.00 36.85  ? 19  PRO   B CA  1 
ATOM   898  C C   . PRO   B 1 20 ? 13.387  -20.210 -29.879 1.00 35.65  ? 19  PRO   B C   1 
ATOM   899  O O   . PRO   B 1 20 ? 14.080  -19.343 -29.332 1.00 35.84  ? 19  PRO   B O   1 
ATOM   900  C CB  . PRO   B 1 20 ? 10.895  -20.159 -29.336 1.00 32.75  ? 19  PRO   B CB  1 
ATOM   901  C CG  . PRO   B 1 20 ? 10.814  -19.257 -28.107 1.00 33.38  ? 19  PRO   B CG  1 
ATOM   902  C CD  . PRO   B 1 20 ? 11.326  -20.144 -26.998 1.00 33.24  ? 19  PRO   B CD  1 
ATOM   903  N N   . HIS   B 1 21 ? 13.541  -20.600 -31.144 1.00 35.04  ? 20  HIS   B N   1 
ATOM   904  C CA  . HIS   B 1 21 ? 14.294  -19.807 -32.101 1.00 32.10  ? 20  HIS   B CA  1 
ATOM   905  C C   . HIS   B 1 21 ? 14.031  -18.331 -31.870 1.00 33.41  ? 20  HIS   B C   1 
ATOM   906  O O   . HIS   B 1 21 ? 12.899  -17.874 -32.014 1.00 34.92  ? 20  HIS   B O   1 
ATOM   907  C CB  . HIS   B 1 21 ? 13.953  -20.264 -33.517 1.00 34.79  ? 20  HIS   B CB  1 
ATOM   908  C CG  . HIS   B 1 21 ? 14.190  -21.726 -33.596 1.00 34.23  ? 20  HIS   B CG  1 
ATOM   909  N ND1 . HIS   B 1 21 ? 13.207  -22.651 -33.342 1.00 37.53  ? 20  HIS   B ND1 1 
ATOM   910  C CD2 . HIS   B 1 21 ? 15.302  -22.421 -33.860 1.00 36.82  ? 20  HIS   B CD2 1 
ATOM   911  C CE1 . HIS   B 1 21 ? 13.709  -23.869 -33.486 1.00 36.39  ? 20  HIS   B CE1 1 
ATOM   912  N NE2 . HIS   B 1 21 ? 14.986  -23.757 -33.779 1.00 38.54  ? 20  HIS   B NE2 1 
ATOM   913  N N   . TRP   B 1 22 ? 15.095  -17.606 -31.501 1.00 34.66  ? 21  TRP   B N   1 
ATOM   914  C CA  . TRP   B 1 22 ? 14.947  -16.263 -30.987 1.00 37.75  ? 21  TRP   B CA  1 
ATOM   915  C C   . TRP   B 1 22 ? 15.489  -15.239 -31.972 1.00 39.14  ? 21  TRP   B C   1 
ATOM   916  O O   . TRP   B 1 22 ? 16.588  -15.423 -32.499 1.00 42.25  ? 21  TRP   B O   1 
ATOM   917  C CB  . TRP   B 1 22 ? 15.669  -16.130 -29.641 1.00 40.13  ? 21  TRP   B CB  1 
ATOM   918  C CG  . TRP   B 1 22 ? 15.114  -14.995 -28.832 1.00 44.41  ? 21  TRP   B CG  1 
ATOM   919  C CD1 . TRP   B 1 22 ? 15.428  -13.673 -28.964 1.00 43.70  ? 21  TRP   B CD1 1 
ATOM   920  C CD2 . TRP   B 1 22 ? 14.122  -15.081 -27.781 1.00 43.97  ? 21  TRP   B CD2 1 
ATOM   921  N NE1 . TRP   B 1 22 ? 14.718  -12.938 -28.050 1.00 49.57  ? 21  TRP   B NE1 1 
ATOM   922  C CE2 . TRP   B 1 22 ? 13.911  -13.769 -27.313 1.00 42.14  ? 21  TRP   B CE2 1 
ATOM   923  C CE3 . TRP   B 1 22 ? 13.408  -16.124 -27.185 1.00 44.12  ? 21  TRP   B CE3 1 
ATOM   924  C CZ2 . TRP   B 1 22 ? 13.014  -13.482 -26.286 1.00 44.90  ? 21  TRP   B CZ2 1 
ATOM   925  C CZ3 . TRP   B 1 22 ? 12.527  -15.842 -26.163 1.00 43.94  ? 21  TRP   B CZ3 1 
ATOM   926  C CH2 . TRP   B 1 22 ? 12.329  -14.534 -25.725 1.00 42.10  ? 21  TRP   B CH2 1 
ATOM   927  N N   . PRO   B 1 23 ? 14.732  -14.140 -32.217 1.00 36.04  ? 22  PRO   B N   1 
ATOM   928  C CA  . PRO   B 1 23 ? 15.187  -13.031 -33.054 1.00 39.66  ? 22  PRO   B CA  1 
ATOM   929  C C   . PRO   B 1 23 ? 16.463  -12.505 -32.430 1.00 40.56  ? 22  PRO   B C   1 
ATOM   930  O O   . PRO   B 1 23 ? 16.474  -12.204 -31.241 1.00 50.64  ? 22  PRO   B O   1 
ATOM   931  C CB  . PRO   B 1 23 ? 14.056  -11.981 -33.056 1.00 37.24  ? 22  PRO   B CB  1 
ATOM   932  C CG  . PRO   B 1 23 ? 13.051  -12.477 -32.041 1.00 35.94  ? 22  PRO   B CG  1 
ATOM   933  C CD  . PRO   B 1 23 ? 13.353  -13.947 -31.764 1.00 38.21  ? 22  PRO   B CD  1 
ATOM   934  N N   . ALA   B 1 24 ? 17.524  -12.452 -33.244 1.00 40.81  ? 23  ALA   B N   1 
ATOM   935  C CA  . ALA   B 1 24 ? 18.856  -12.044 -32.834 1.00 35.70  ? 23  ALA   B CA  1 
ATOM   936  C C   . ALA   B 1 24 ? 19.637  -11.532 -34.046 1.00 39.87  ? 23  ALA   B C   1 
ATOM   937  O O   . ALA   B 1 24 ? 19.173  -11.648 -35.184 1.00 37.53  ? 23  ALA   B O   1 
ATOM   938  C CB  . ALA   B 1 24 ? 19.559  -13.209 -32.185 1.00 38.75  ? 23  ALA   B CB  1 
ATOM   939  N N   . ARG   B 1 25 ? 20.836  -10.996 -33.759 1.00 38.12  ? 24  ARG   B N   1 
ATOM   940  C CA  . ARG   B 1 25 ? 21.780  -10.465 -34.731 1.00 43.71  ? 24  ARG   B CA  1 
ATOM   941  C C   . ARG   B 1 25 ? 23.193  -10.950 -34.403 1.00 42.73  ? 24  ARG   B C   1 
ATOM   942  O O   . ARG   B 1 25 ? 23.546  -11.199 -33.234 1.00 39.55  ? 24  ARG   B O   1 
ATOM   943  C CB  . ARG   B 1 25 ? 21.754  -8.929  -34.819 1.00 41.89  ? 24  ARG   B CB  1 
ATOM   944  C CG  . ARG   B 1 25 ? 22.313  -8.136  -33.643 1.00 48.81  ? 24  ARG   B CG  1 
ATOM   945  C CD  . ARG   B 1 25 ? 22.427  -6.629  -33.909 1.00 45.23  ? 24  ARG   B CD  1 
ATOM   946  N NE  . ARG   B 1 25 ? 22.940  -5.819  -32.792 1.00 42.28  ? 24  ARG   B NE  1 
ATOM   947  C CZ  . ARG   B 1 25 ? 22.482  -4.614  -32.473 1.00 43.30  ? 24  ARG   B CZ  1 
ATOM   948  N NH1 . ARG   B 1 25 ? 21.561  -4.069  -33.246 1.00 41.24  ? 24  ARG   B NH1 1 
ATOM   949  N NH2 . ARG   B 1 25 ? 22.939  -3.967  -31.411 1.00 37.12  ? 24  ARG   B NH2 1 
ATOM   950  N N   . ILE   B 1 26 ? 24.002  -11.084 -35.461 1.00 40.72  ? 25  ILE   B N   1 
ATOM   951  C CA  . ILE   B 1 26 ? 25.441  -11.237 -35.293 1.00 42.85  ? 25  ILE   B CA  1 
ATOM   952  C C   . ILE   B 1 26 ? 26.022  -9.861  -34.960 1.00 43.67  ? 25  ILE   B C   1 
ATOM   953  O O   . ILE   B 1 26 ? 25.901  -8.940  -35.754 1.00 44.41  ? 25  ILE   B O   1 
ATOM   954  C CB  . ILE   B 1 26 ? 26.111  -11.815 -36.560 1.00 43.67  ? 25  ILE   B CB  1 
ATOM   955  C CG1 . ILE   B 1 26 ? 25.423  -13.100 -37.133 1.00 41.35  ? 25  ILE   B CG1 1 
ATOM   956  C CG2 . ILE   B 1 26 ? 27.628  -11.976 -36.359 1.00 44.86  ? 25  ILE   B CG2 1 
ATOM   957  C CD1 . ILE   B 1 26 ? 25.244  -14.277 -36.175 1.00 40.07  ? 25  ILE   B CD1 1 
ATOM   958  N N   . ASP   B 1 27 ? 26.658  -9.740  -33.791 1.00 48.37  ? 26  ASP   B N   1 
ATOM   959  C CA  . ASP   B 1 27 ? 27.391  -8.548  -33.392 1.00 50.74  ? 26  ASP   B CA  1 
ATOM   960  C C   . ASP   B 1 27 ? 28.858  -8.601  -33.831 1.00 57.58  ? 26  ASP   B C   1 
ATOM   961  O O   . ASP   B 1 27 ? 29.356  -9.657  -34.218 1.00 55.85  ? 26  ASP   B O   1 
ATOM   962  C CB  . ASP   B 1 27 ? 27.380  -8.455  -31.879 1.00 48.86  ? 26  ASP   B CB  1 
ATOM   963  C CG  . ASP   B 1 27 ? 26.217  -7.661  -31.325 1.00 50.28  ? 26  ASP   B CG  1 
ATOM   964  O OD1 . ASP   B 1 27 ? 25.410  -7.187  -32.154 1.00 43.17  ? 26  ASP   B OD1 1 
ATOM   965  O OD2 . ASP   B 1 27 ? 26.171  -7.482  -30.085 1.00 46.75  ? 26  ASP   B OD2 1 
ATOM   966  N N   A ASP   B 1 28 ? 29.548  -7.453  -33.711 0.51 61.33  ? 27  ASP   B N   1 
ATOM   967  N N   B ASP   B 1 28 ? 29.532  -7.443  -33.755 0.49 61.85  ? 27  ASP   B N   1 
ATOM   968  C CA  A ASP   B 1 28 ? 30.977  -7.319  -33.967 0.51 57.26  ? 27  ASP   B CA  1 
ATOM   969  C CA  B ASP   B 1 28 ? 30.977  -7.324  -33.888 0.49 58.33  ? 27  ASP   B CA  1 
ATOM   970  C C   A ASP   B 1 28 ? 31.757  -7.941  -32.803 0.51 54.63  ? 27  ASP   B C   1 
ATOM   971  C C   B ASP   B 1 28 ? 31.631  -7.780  -32.580 0.49 54.11  ? 27  ASP   B C   1 
ATOM   972  O O   A ASP   B 1 28 ? 31.323  -7.720  -31.643 0.51 51.33  ? 27  ASP   B O   1 
ATOM   973  O O   B ASP   B 1 28 ? 30.997  -7.532  -31.525 0.49 45.74  ? 27  ASP   B O   1 
ATOM   974  C CB  A ASP   B 1 28 ? 31.393  -5.859  -34.081 0.51 60.87  ? 27  ASP   B CB  1 
ATOM   975  C CB  B ASP   B 1 28 ? 31.380  -5.882  -34.159 0.49 64.85  ? 27  ASP   B CB  1 
ATOM   976  C CG  A ASP   B 1 28 ? 30.307  -4.882  -34.513 0.51 58.13  ? 27  ASP   B CG  1 
ATOM   977  C CG  B ASP   B 1 28 ? 31.034  -5.356  -35.543 0.49 64.40  ? 27  ASP   B CG  1 
ATOM   978  O OD1 A ASP   B 1 28 ? 30.344  -4.447  -35.683 0.51 56.82  ? 27  ASP   B OD1 1 
ATOM   979  O OD1 B ASP   B 1 28 ? 31.760  -5.713  -36.489 0.49 66.18  ? 27  ASP   B OD1 1 
ATOM   980  O OD2 A ASP   B 1 28 ? 29.441  -4.557  -33.668 0.51 53.91  ? 27  ASP   B OD2 1 
ATOM   981  O OD2 B ASP   B 1 28 ? 30.031  -4.618  -35.665 0.49 63.85  ? 27  ASP   B OD2 1 
ATOM   982  N N   . VAL   B 1 34 ? 35.612  -10.216 -24.383 1.00 73.17  ? 33  VAL   B N   1 
ATOM   983  C CA  . VAL   B 1 34 ? 36.284  -11.539 -24.576 1.00 78.59  ? 33  VAL   B CA  1 
ATOM   984  C C   . VAL   B 1 34 ? 35.944  -12.045 -25.973 1.00 83.48  ? 33  VAL   B C   1 
ATOM   985  O O   . VAL   B 1 34 ? 34.762  -12.196 -26.276 1.00 84.46  ? 33  VAL   B O   1 
ATOM   986  C CB  . VAL   B 1 34 ? 35.874  -12.571 -23.505 1.00 80.24  ? 33  VAL   B CB  1 
ATOM   987  C CG1 . VAL   B 1 34 ? 34.360  -12.740 -23.402 1.00 67.85  ? 33  VAL   B CG1 1 
ATOM   988  C CG2 . VAL   B 1 34 ? 36.558  -13.921 -23.732 1.00 83.34  ? 33  VAL   B CG2 1 
ATOM   989  N N   . LYS   B 1 35 ? 36.978  -12.325 -26.788 1.00 83.28  ? 34  LYS   B N   1 
ATOM   990  C CA  . LYS   B 1 35 ? 36.813  -12.793 -28.164 1.00 83.80  ? 34  LYS   B CA  1 
ATOM   991  C C   . LYS   B 1 35 ? 36.080  -14.138 -28.178 1.00 83.55  ? 34  LYS   B C   1 
ATOM   992  O O   . LYS   B 1 35 ? 36.298  -14.972 -27.296 1.00 89.47  ? 34  LYS   B O   1 
ATOM   993  C CB  . LYS   B 1 35 ? 38.135  -12.873 -28.944 1.00 68.41  ? 34  LYS   B CB  1 
ATOM   994  N N   . PRO   B 1 36 ? 35.172  -14.384 -29.161 1.00 81.80  ? 35  PRO   B N   1 
ATOM   995  C CA  . PRO   B 1 36 ? 34.380  -15.624 -29.197 1.00 76.62  ? 35  PRO   B CA  1 
ATOM   996  C C   . PRO   B 1 36 ? 35.193  -16.915 -29.270 1.00 67.86  ? 35  PRO   B C   1 
ATOM   997  O O   . PRO   B 1 36 ? 36.303  -16.916 -29.800 1.00 65.97  ? 35  PRO   B O   1 
ATOM   998  C CB  . PRO   B 1 36 ? 33.468  -15.441 -30.432 1.00 77.10  ? 35  PRO   B CB  1 
ATOM   999  C CG  . PRO   B 1 36 ? 34.188  -14.403 -31.286 1.00 78.92  ? 35  PRO   B CG  1 
ATOM   1000 C CD  . PRO   B 1 36 ? 34.843  -13.471 -30.274 1.00 78.83  ? 35  PRO   B CD  1 
ATOM   1001 N N   . PRO   B 1 37 ? 34.671  -18.050 -28.746 1.00 65.02  ? 36  PRO   B N   1 
ATOM   1002 C CA  . PRO   B 1 37 ? 35.303  -19.353 -28.950 1.00 64.75  ? 36  PRO   B CA  1 
ATOM   1003 C C   . PRO   B 1 37 ? 35.357  -19.634 -30.450 1.00 77.86  ? 36  PRO   B C   1 
ATOM   1004 O O   . PRO   B 1 37 ? 34.685  -18.969 -31.240 1.00 72.00  ? 36  PRO   B O   1 
ATOM   1005 C CB  . PRO   B 1 37 ? 34.383  -20.354 -28.226 1.00 62.26  ? 36  PRO   B CB  1 
ATOM   1006 C CG  . PRO   B 1 37 ? 33.567  -19.505 -27.282 1.00 64.62  ? 36  PRO   B CG  1 
ATOM   1007 C CD  . PRO   B 1 37 ? 33.441  -18.141 -27.946 1.00 65.70  ? 36  PRO   B CD  1 
ATOM   1008 N N   . PRO   B 1 38 ? 36.162  -20.629 -30.895 1.00 90.46  ? 37  PRO   B N   1 
ATOM   1009 C CA  . PRO   B 1 38 ? 36.201  -21.010 -32.311 1.00 83.26  ? 37  PRO   B CA  1 
ATOM   1010 C C   . PRO   B 1 38 ? 34.829  -21.459 -32.801 1.00 76.17  ? 37  PRO   B C   1 
ATOM   1011 O O   . PRO   B 1 38 ? 33.978  -21.837 -31.994 1.00 79.48  ? 37  PRO   B O   1 
ATOM   1012 C CB  . PRO   B 1 38 ? 37.220  -22.159 -32.342 1.00 88.13  ? 37  PRO   B CB  1 
ATOM   1013 C CG  . PRO   B 1 38 ? 38.062  -21.948 -31.097 1.00 94.09  ? 37  PRO   B CG  1 
ATOM   1014 C CD  . PRO   B 1 38 ? 37.093  -21.409 -30.061 1.00 89.84  ? 37  PRO   B CD  1 
ATOM   1015 N N   . ASN   B 1 39 ? 34.635  -21.393 -34.127 1.00 65.82  ? 38  ASN   B N   1 
ATOM   1016 C CA  . ASN   B 1 39 ? 33.445  -21.887 -34.808 1.00 61.46  ? 38  ASN   B CA  1 
ATOM   1017 C C   . ASN   B 1 39 ? 32.170  -21.260 -34.239 1.00 63.72  ? 38  ASN   B C   1 
ATOM   1018 O O   . ASN   B 1 39 ? 31.102  -21.845 -34.359 1.00 72.43  ? 38  ASN   B O   1 
ATOM   1019 C CB  . ASN   B 1 39 ? 33.299  -23.407 -34.736 1.00 63.28  ? 38  ASN   B CB  1 
ATOM   1020 C CG  . ASN   B 1 39 ? 34.592  -24.179 -34.877 1.00 75.79  ? 38  ASN   B CG  1 
ATOM   1021 O OD1 . ASN   B 1 39 ? 34.817  -25.135 -34.126 1.00 80.82  ? 38  ASN   B OD1 1 
ATOM   1022 N ND2 . ASN   B 1 39 ? 35.437  -23.820 -35.836 1.00 80.94  ? 38  ASN   B ND2 1 
ATOM   1023 N N   . LYS   B 1 40 ? 32.268  -20.079 -33.614 1.00 69.94  ? 39  LYS   B N   1 
ATOM   1024 C CA  . LYS   B 1 40 ? 31.120  -19.445 -32.975 1.00 61.55  ? 39  LYS   B CA  1 
ATOM   1025 C C   . LYS   B 1 40 ? 31.164  -17.925 -33.155 1.00 57.81  ? 39  LYS   B C   1 
ATOM   1026 O O   . LYS   B 1 40 ? 32.233  -17.318 -33.242 1.00 56.24  ? 39  LYS   B O   1 
ATOM   1027 C CB  . LYS   B 1 40 ? 31.071  -19.785 -31.482 1.00 62.78  ? 39  LYS   B CB  1 
ATOM   1028 C CG  . LYS   B 1 40 ? 31.165  -21.257 -31.082 1.00 56.78  ? 39  LYS   B CG  1 
ATOM   1029 C CD  . LYS   B 1 40 ? 31.093  -21.408 -29.565 1.00 55.58  ? 39  LYS   B CD  1 
ATOM   1030 C CE  . LYS   B 1 40 ? 29.722  -21.385 -28.957 1.00 62.10  ? 39  LYS   B CE  1 
ATOM   1031 N NZ  . LYS   B 1 40 ? 29.134  -22.715 -28.749 1.00 64.07  ? 39  LYS   B NZ  1 
ATOM   1032 N N   . TYR   B 1 41 ? 29.983  -17.305 -33.206 1.00 48.80  ? 40  TYR   B N   1 
ATOM   1033 C CA  . TYR   B 1 41 ? 29.919  -15.868 -33.330 1.00 47.21  ? 40  TYR   B CA  1 
ATOM   1034 C C   . TYR   B 1 41 ? 29.378  -15.269 -32.038 1.00 55.06  ? 40  TYR   B C   1 
ATOM   1035 O O   . TYR   B 1 41 ? 28.819  -15.982 -31.199 1.00 58.01  ? 40  TYR   B O   1 
ATOM   1036 C CB  . TYR   B 1 41 ? 28.981  -15.572 -34.493 1.00 50.95  ? 40  TYR   B CB  1 
ATOM   1037 C CG  . TYR   B 1 41 ? 29.450  -16.168 -35.805 1.00 50.22  ? 40  TYR   B CG  1 
ATOM   1038 C CD1 . TYR   B 1 41 ? 29.771  -15.348 -36.873 1.00 53.21  ? 40  TYR   B CD1 1 
ATOM   1039 C CD2 . TYR   B 1 41 ? 29.564  -17.538 -35.974 1.00 54.96  ? 40  TYR   B CD2 1 
ATOM   1040 C CE1 . TYR   B 1 41 ? 30.194  -15.875 -38.080 1.00 56.05  ? 40  TYR   B CE1 1 
ATOM   1041 C CE2 . TYR   B 1 41 ? 29.997  -18.080 -37.175 1.00 64.18  ? 40  TYR   B CE2 1 
ATOM   1042 C CZ  . TYR   B 1 41 ? 30.303  -17.242 -38.232 1.00 59.51  ? 40  TYR   B CZ  1 
ATOM   1043 O OH  . TYR   B 1 41 ? 30.721  -17.738 -39.427 1.00 67.76  ? 40  TYR   B OH  1 
ATOM   1044 N N   . PRO   B 1 42 ? 29.532  -13.936 -31.842 1.00 50.42  ? 41  PRO   B N   1 
ATOM   1045 C CA  . PRO   B 1 42 ? 28.834  -13.238 -30.769 1.00 49.06  ? 41  PRO   B CA  1 
ATOM   1046 C C   . PRO   B 1 42 ? 27.421  -12.882 -31.223 1.00 51.31  ? 41  PRO   B C   1 
ATOM   1047 O O   . PRO   B 1 42 ? 27.214  -12.311 -32.296 1.00 55.27  ? 41  PRO   B O   1 
ATOM   1048 C CB  . PRO   B 1 42 ? 29.722  -12.015 -30.508 1.00 46.70  ? 41  PRO   B CB  1 
ATOM   1049 C CG  . PRO   B 1 42 ? 30.404  -11.739 -31.838 1.00 49.08  ? 41  PRO   B CG  1 
ATOM   1050 C CD  . PRO   B 1 42 ? 30.411  -13.043 -32.615 1.00 49.18  ? 41  PRO   B CD  1 
ATOM   1051 N N   . ILE   B 1 43 ? 26.453  -13.230 -30.374 1.00 52.25  ? 42  ILE   B N   1 
ATOM   1052 C CA  . ILE   B 1 43 ? 25.044  -13.088 -30.693 1.00 49.91  ? 42  ILE   B CA  1 
ATOM   1053 C C   . ILE   B 1 43 ? 24.401  -12.031 -29.796 1.00 47.75  ? 42  ILE   B C   1 
ATOM   1054 O O   . ILE   B 1 43 ? 24.501  -12.096 -28.570 1.00 45.96  ? 42  ILE   B O   1 
ATOM   1055 C CB  . ILE   B 1 43 ? 24.347  -14.450 -30.555 1.00 45.96  ? 42  ILE   B CB  1 
ATOM   1056 C CG1 . ILE   B 1 43 ? 25.077  -15.528 -31.365 1.00 43.98  ? 42  ILE   B CG1 1 
ATOM   1057 C CG2 . ILE   B 1 43 ? 22.871  -14.335 -30.938 1.00 53.02  ? 42  ILE   B CG2 1 
ATOM   1058 C CD1 . ILE   B 1 43 ? 25.363  -15.140 -32.810 1.00 36.57  ? 42  ILE   B CD1 1 
ATOM   1059 N N   . PHE   B 1 44 ? 23.727  -11.068 -30.433 1.00 41.22  ? 43  PHE   B N   1 
ATOM   1060 C CA  . PHE   B 1 44 ? 22.858  -10.156 -29.707 1.00 42.92  ? 43  PHE   B CA  1 
ATOM   1061 C C   . PHE   B 1 44 ? 21.423  -10.642 -29.883 1.00 41.61  ? 43  PHE   B C   1 
ATOM   1062 O O   . PHE   B 1 44 ? 20.995  -10.870 -31.025 1.00 40.02  ? 43  PHE   B O   1 
ATOM   1063 C CB  . PHE   B 1 44 ? 22.983  -8.702  -30.182 1.00 41.53  ? 43  PHE   B CB  1 
ATOM   1064 C CG  . PHE   B 1 44 ? 22.035  -7.761  -29.451 1.00 44.93  ? 43  PHE   B CG  1 
ATOM   1065 C CD1 . PHE   B 1 44 ? 20.823  -7.381  -30.021 1.00 47.41  ? 43  PHE   B CD1 1 
ATOM   1066 C CD2 . PHE   B 1 44 ? 22.341  -7.283  -28.174 1.00 51.06  ? 43  PHE   B CD2 1 
ATOM   1067 C CE1 . PHE   B 1 44 ? 19.953  -6.534  -29.343 1.00 48.82  ? 43  PHE   B CE1 1 
ATOM   1068 C CE2 . PHE   B 1 44 ? 21.476  -6.429  -27.504 1.00 47.77  ? 43  PHE   B CE2 1 
ATOM   1069 C CZ  . PHE   B 1 44 ? 20.277  -6.068  -28.083 1.00 50.03  ? 43  PHE   B CZ  1 
ATOM   1070 N N   . PHE   B 1 45 ? 20.711  -10.820 -28.754 1.00 38.36  ? 44  PHE   B N   1 
ATOM   1071 C CA  . PHE   B 1 45 ? 19.303  -11.224 -28.755 1.00 40.72  ? 44  PHE   B CA  1 
ATOM   1072 C C   . PHE   B 1 45 ? 18.391  -10.007 -28.587 1.00 38.61  ? 44  PHE   B C   1 
ATOM   1073 O O   . PHE   B 1 45 ? 18.398  -9.365  -27.539 1.00 48.93  ? 44  PHE   B O   1 
ATOM   1074 C CB  . PHE   B 1 45 ? 18.953  -12.261 -27.679 1.00 36.84  ? 44  PHE   B CB  1 
ATOM   1075 C CG  . PHE   B 1 45 ? 19.646  -13.608 -27.795 1.00 35.34  ? 44  PHE   B CG  1 
ATOM   1076 C CD1 . PHE   B 1 45 ? 20.901  -13.818 -27.237 1.00 35.92  ? 44  PHE   B CD1 1 
ATOM   1077 C CD2 . PHE   B 1 45 ? 19.033  -14.671 -28.446 1.00 38.69  ? 44  PHE   B CD2 1 
ATOM   1078 C CE1 . PHE   B 1 45 ? 21.518  -15.056 -27.334 1.00 39.65  ? 44  PHE   B CE1 1 
ATOM   1079 C CE2 . PHE   B 1 45 ? 19.665  -15.903 -28.557 1.00 38.11  ? 44  PHE   B CE2 1 
ATOM   1080 C CZ  . PHE   B 1 45 ? 20.901  -16.092 -27.994 1.00 36.75  ? 44  PHE   B CZ  1 
ATOM   1081 N N   . PHE   B 1 46 ? 17.605  -9.684  -29.623 1.00 38.11  ? 45  PHE   B N   1 
ATOM   1082 C CA  . PHE   B 1 46 ? 16.631  -8.604  -29.534 1.00 39.74  ? 45  PHE   B CA  1 
ATOM   1083 C C   . PHE   B 1 46 ? 15.643  -8.912  -28.404 1.00 41.78  ? 45  PHE   B C   1 
ATOM   1084 O O   . PHE   B 1 46 ? 15.572  -10.052 -27.954 1.00 47.31  ? 45  PHE   B O   1 
ATOM   1085 C CB  . PHE   B 1 46 ? 15.881  -8.471  -30.860 1.00 36.42  ? 45  PHE   B CB  1 
ATOM   1086 C CG  . PHE   B 1 46 ? 16.792  -8.037  -31.993 1.00 41.65  ? 45  PHE   B CG  1 
ATOM   1087 C CD1 . PHE   B 1 46 ? 17.335  -6.754  -32.019 1.00 45.93  ? 45  PHE   B CD1 1 
ATOM   1088 C CD2 . PHE   B 1 46 ? 17.093  -8.896  -33.041 1.00 40.97  ? 45  PHE   B CD2 1 
ATOM   1089 C CE1 . PHE   B 1 46 ? 18.156  -6.343  -33.064 1.00 41.56  ? 45  PHE   B CE1 1 
ATOM   1090 C CE2 . PHE   B 1 46 ? 17.948  -8.490  -34.059 1.00 48.25  ? 45  PHE   B CE2 1 
ATOM   1091 C CZ  . PHE   B 1 46 ? 18.458  -7.207  -34.084 1.00 42.67  ? 45  PHE   B CZ  1 
ATOM   1092 N N   . GLY   B 1 47 ? 14.869  -7.903  -27.974 1.00 38.48  ? 46  GLY   B N   1 
ATOM   1093 C CA  . GLY   B 1 47 ? 13.890  -8.063  -26.907 1.00 39.06  ? 46  GLY   B CA  1 
ATOM   1094 C C   . GLY   B 1 47 ? 14.547  -8.066  -25.526 1.00 37.60  ? 46  GLY   B C   1 
ATOM   1095 O O   . GLY   B 1 47 ? 14.439  -7.106  -24.783 1.00 43.91  ? 46  GLY   B O   1 
ATOM   1096 N N   . THR   B 1 48 ? 15.256  -9.144  -25.205 1.00 40.45  ? 47  THR   B N   1 
ATOM   1097 C CA  . THR   B 1 48 ? 15.895  -9.297  -23.912 1.00 38.74  ? 47  THR   B CA  1 
ATOM   1098 C C   . THR   B 1 48 ? 17.232  -8.549  -23.903 1.00 39.73  ? 47  THR   B C   1 
ATOM   1099 O O   . THR   B 1 48 ? 17.741  -8.216  -22.838 1.00 35.61  ? 47  THR   B O   1 
ATOM   1100 C CB  . THR   B 1 48 ? 16.107  -10.786 -23.627 1.00 37.98  ? 47  THR   B CB  1 
ATOM   1101 O OG1 . THR   B 1 48 ? 17.123  -11.140 -24.555 1.00 39.21  ? 47  THR   B OG1 1 
ATOM   1102 C CG2 . THR   B 1 48 ? 14.873  -11.652 -23.802 1.00 37.96  ? 47  THR   B CG2 1 
ATOM   1103 N N   . HIS   B 1 49 ? 17.842  -8.369  -25.081 1.00 37.98  ? 48  HIS   B N   1 
ATOM   1104 C CA  . HIS   B 1 49 ? 19.108  -7.660  -25.213 1.00 44.42  ? 48  HIS   B CA  1 
ATOM   1105 C C   . HIS   B 1 49 ? 20.200  -8.366  -24.429 1.00 47.21  ? 48  HIS   B C   1 
ATOM   1106 O O   . HIS   B 1 49 ? 21.154  -7.725  -24.002 1.00 50.41  ? 48  HIS   B O   1 
ATOM   1107 C CB  . HIS   B 1 49 ? 18.991  -6.173  -24.847 1.00 42.58  ? 48  HIS   B CB  1 
ATOM   1108 C CG  . HIS   B 1 49 ? 17.833  -5.572  -25.542 1.00 41.11  ? 48  HIS   B CG  1 
ATOM   1109 N ND1 . HIS   B 1 49 ? 16.755  -5.065  -24.859 1.00 45.20  ? 48  HIS   B ND1 1 
ATOM   1110 C CD2 . HIS   B 1 49 ? 17.510  -5.530  -26.844 1.00 41.55  ? 48  HIS   B CD2 1 
ATOM   1111 C CE1 . HIS   B 1 49 ? 15.837  -4.667  -25.737 1.00 53.25  ? 48  HIS   B CE1 1 
ATOM   1112 N NE2 . HIS   B 1 49 ? 16.268  -4.962  -26.952 1.00 43.96  ? 48  HIS   B NE2 1 
ATOM   1113 N N   . GLU   B 1 50 ? 20.051  -9.685  -24.277 1.00 49.87  ? 49  GLU   B N   1 
ATOM   1114 C CA  . GLU   B 1 50 ? 21.126  -10.530 -23.783 1.00 49.52  ? 49  GLU   B CA  1 
ATOM   1115 C C   . GLU   B 1 50 ? 22.119  -10.862 -24.898 1.00 47.12  ? 49  GLU   B C   1 
ATOM   1116 O O   . GLU   B 1 50 ? 21.905  -10.535 -26.073 1.00 47.89  ? 49  GLU   B O   1 
ATOM   1117 C CB  . GLU   B 1 50 ? 20.534  -11.808 -23.193 1.00 60.11  ? 49  GLU   B CB  1 
ATOM   1118 C CG  . GLU   B 1 50 ? 19.625  -11.519 -21.999 1.00 65.94  ? 49  GLU   B CG  1 
ATOM   1119 C CD  . GLU   B 1 50 ? 19.567  -12.651 -20.994 1.00 65.72  ? 49  GLU   B CD  1 
ATOM   1120 O OE1 . GLU   B 1 50 ? 18.491  -13.239 -20.772 1.00 69.98  ? 49  GLU   B OE1 1 
ATOM   1121 O OE2 . GLU   B 1 50 ? 20.636  -12.952 -20.434 1.00 73.48  ? 49  GLU   B OE2 1 
ATOM   1122 N N   . THR   B 1 51 ? 23.219  -11.523 -24.514 1.00 40.81  ? 50  THR   B N   1 
ATOM   1123 C CA  . THR   B 1 51 ? 24.235  -11.952 -25.466 1.00 40.63  ? 50  THR   B CA  1 
ATOM   1124 C C   . THR   B 1 51 ? 24.634  -13.380 -25.119 1.00 42.54  ? 50  THR   B C   1 
ATOM   1125 O O   . THR   B 1 51 ? 24.602  -13.775 -23.956 1.00 44.08  ? 50  THR   B O   1 
ATOM   1126 C CB  . THR   B 1 51 ? 25.457  -11.019 -25.460 1.00 43.76  ? 50  THR   B CB  1 
ATOM   1127 O OG1 . THR   B 1 51 ? 25.998  -11.073 -24.144 1.00 55.16  ? 50  THR   B OG1 1 
ATOM   1128 C CG2 . THR   B 1 51 ? 25.149  -9.557  -25.748 1.00 40.84  ? 50  THR   B CG2 1 
ATOM   1129 N N   . ALA   B 1 52 ? 25.023  -14.151 -26.138 1.00 39.16  ? 51  ALA   B N   1 
ATOM   1130 C CA  . ALA   B 1 52 ? 25.655  -15.445 -25.941 1.00 34.81  ? 51  ALA   B CA  1 
ATOM   1131 C C   . ALA   B 1 52 ? 26.496  -15.738 -27.170 1.00 39.41  ? 51  ALA   B C   1 
ATOM   1132 O O   . ALA   B 1 52 ? 26.293  -15.134 -28.220 1.00 46.14  ? 51  ALA   B O   1 
ATOM   1133 C CB  . ALA   B 1 52 ? 24.617  -16.538 -25.741 1.00 37.09  ? 51  ALA   B CB  1 
ATOM   1134 N N   . PHE   B 1 53 ? 27.427  -16.678 -27.023 1.00 46.74  ? 52  PHE   B N   1 
ATOM   1135 C CA  . PHE   B 1 53 ? 28.111  -17.259 -28.162 1.00 49.05  ? 52  PHE   B CA  1 
ATOM   1136 C C   . PHE   B 1 53 ? 27.254  -18.414 -28.664 1.00 46.48  ? 52  PHE   B C   1 
ATOM   1137 O O   . PHE   B 1 53 ? 26.670  -19.125 -27.845 1.00 46.25  ? 52  PHE   B O   1 
ATOM   1138 C CB  . PHE   B 1 53 ? 29.525  -17.668 -27.740 1.00 53.21  ? 52  PHE   B CB  1 
ATOM   1139 C CG  . PHE   B 1 53 ? 30.340  -16.489 -27.227 1.00 54.84  ? 52  PHE   B CG  1 
ATOM   1140 C CD1 . PHE   B 1 53 ? 30.643  -15.420 -28.063 1.00 56.90  ? 52  PHE   B CD1 1 
ATOM   1141 C CD2 . PHE   B 1 53 ? 30.787  -16.446 -25.907 1.00 57.61  ? 52  PHE   B CD2 1 
ATOM   1142 C CE1 . PHE   B 1 53 ? 31.357  -14.333 -27.583 1.00 59.05  ? 52  PHE   B CE1 1 
ATOM   1143 C CE2 . PHE   B 1 53 ? 31.510  -15.359 -25.434 1.00 54.64  ? 52  PHE   B CE2 1 
ATOM   1144 C CZ  . PHE   B 1 53 ? 31.796  -14.308 -26.274 1.00 56.54  ? 52  PHE   B CZ  1 
ATOM   1145 N N   . LEU   B 1 54 ? 27.114  -18.506 -30.000 1.00 42.75  ? 53  LEU   B N   1 
ATOM   1146 C CA  . LEU   B 1 54 ? 26.369  -19.566 -30.666 1.00 45.55  ? 53  LEU   B CA  1 
ATOM   1147 C C   . LEU   B 1 54 ? 27.100  -19.928 -31.954 1.00 48.32  ? 53  LEU   B C   1 
ATOM   1148 O O   . LEU   B 1 54 ? 27.673  -19.043 -32.594 1.00 46.10  ? 53  LEU   B O   1 
ATOM   1149 C CB  . LEU   B 1 54 ? 24.905  -19.211 -30.959 1.00 43.97  ? 53  LEU   B CB  1 
ATOM   1150 C CG  . LEU   B 1 54 ? 23.912  -19.338 -29.796 1.00 43.25  ? 53  LEU   B CG  1 
ATOM   1151 C CD1 . LEU   B 1 54 ? 22.514  -18.972 -30.267 1.00 42.36  ? 53  LEU   B CD1 1 
ATOM   1152 C CD2 . LEU   B 1 54 ? 23.910  -20.727 -29.177 1.00 34.55  ? 53  LEU   B CD2 1 
ATOM   1153 N N   . GLY   B 1 55 ? 27.059  -21.222 -32.315 1.00 44.27  ? 54  GLY   B N   1 
ATOM   1154 C CA  . GLY   B 1 55 ? 27.667  -21.705 -33.548 1.00 42.93  ? 54  GLY   B CA  1 
ATOM   1155 C C   . GLY   B 1 55 ? 26.635  -21.747 -34.675 1.00 44.23  ? 54  GLY   B C   1 
ATOM   1156 O O   . GLY   B 1 55 ? 25.434  -21.738 -34.403 1.00 47.07  ? 54  GLY   B O   1 
ATOM   1157 N N   . PRO   B 1 56 ? 27.043  -21.804 -35.968 1.00 40.97  ? 55  PRO   B N   1 
ATOM   1158 C CA  . PRO   B 1 56 ? 26.079  -21.790 -37.064 1.00 37.82  ? 55  PRO   B CA  1 
ATOM   1159 C C   . PRO   B 1 56 ? 24.929  -22.800 -37.014 1.00 41.40  ? 55  PRO   B C   1 
ATOM   1160 O O   . PRO   B 1 56 ? 23.908  -22.550 -37.658 1.00 41.56  ? 55  PRO   B O   1 
ATOM   1161 C CB  . PRO   B 1 56 ? 26.982  -21.982 -38.305 1.00 41.03  ? 55  PRO   B CB  1 
ATOM   1162 C CG  . PRO   B 1 56 ? 28.302  -21.394 -37.884 1.00 40.12  ? 55  PRO   B CG  1 
ATOM   1163 C CD  . PRO   B 1 56 ? 28.434  -21.881 -36.443 1.00 39.87  ? 55  PRO   B CD  1 
ATOM   1164 N N   . LYS   B 1 57 ? 25.077  -23.918 -36.264 1.00 40.88  ? 56  LYS   B N   1 
ATOM   1165 C CA  . LYS   B 1 57 ? 24.048  -24.959 -36.221 1.00 44.17  ? 56  LYS   B CA  1 
ATOM   1166 C C   . LYS   B 1 57 ? 22.769  -24.430 -35.549 1.00 46.61  ? 56  LYS   B C   1 
ATOM   1167 O O   . LYS   B 1 57 ? 21.674  -24.990 -35.726 1.00 39.76  ? 56  LYS   B O   1 
ATOM   1168 C CB  . LYS   B 1 57 ? 24.479  -26.318 -35.656 1.00 39.10  ? 56  LYS   B CB  1 
ATOM   1169 C CG  . LYS   B 1 57 ? 24.365  -26.451 -34.149 1.00 39.80  ? 56  LYS   B CG  1 
ATOM   1170 C CD  . LYS   B 1 57 ? 24.329  -27.877 -33.625 1.00 43.65  ? 56  LYS   B CD  1 
ATOM   1171 C CE  . LYS   B 1 57 ? 24.619  -27.946 -32.141 1.00 46.31  ? 56  LYS   B CE  1 
ATOM   1172 N NZ  . LYS   B 1 57 ? 23.424  -27.757 -31.319 1.00 46.53  ? 56  LYS   B NZ  1 
ATOM   1173 N N   . ASP   B 1 58 ? 22.934  -23.335 -34.799 1.00 40.45  ? 57  ASP   B N   1 
ATOM   1174 C CA  . ASP   B 1 58 ? 21.858  -22.708 -34.051 1.00 45.30  ? 57  ASP   B CA  1 
ATOM   1175 C C   . ASP   B 1 58 ? 21.631  -21.290 -34.558 1.00 42.27  ? 57  ASP   B C   1 
ATOM   1176 O O   . ASP   B 1 58 ? 21.206  -20.418 -33.805 1.00 48.24  ? 57  ASP   B O   1 
ATOM   1177 C CB  . ASP   B 1 58 ? 22.192  -22.626 -32.565 1.00 44.19  ? 57  ASP   B CB  1 
ATOM   1178 C CG  . ASP   B 1 58 ? 22.388  -23.961 -31.868 1.00 41.60  ? 57  ASP   B CG  1 
ATOM   1179 O OD1 . ASP   B 1 58 ? 21.507  -24.803 -32.012 1.00 37.17  ? 57  ASP   B OD1 1 
ATOM   1180 O OD2 . ASP   B 1 58 ? 23.419  -24.137 -31.179 1.00 45.99  ? 57  ASP   B OD2 1 
ATOM   1181 N N   . LEU   B 1 59 ? 21.916  -21.056 -35.840 1.00 39.50  ? 58  LEU   B N   1 
ATOM   1182 C CA  . LEU   B 1 59 ? 21.809  -19.710 -36.354 1.00 36.28  ? 58  LEU   B CA  1 
ATOM   1183 C C   . LEU   B 1 59 ? 21.072  -19.786 -37.674 1.00 34.55  ? 58  LEU   B C   1 
ATOM   1184 O O   . LEU   B 1 59 ? 21.554  -20.424 -38.601 1.00 33.96  ? 58  LEU   B O   1 
ATOM   1185 C CB  . LEU   B 1 59 ? 23.192  -19.075 -36.514 1.00 44.05  ? 58  LEU   B CB  1 
ATOM   1186 C CG  . LEU   B 1 59 ? 23.954  -18.727 -35.231 1.00 41.61  ? 58  LEU   B CG  1 
ATOM   1187 C CD1 . LEU   B 1 59 ? 25.322  -18.135 -35.580 1.00 39.19  ? 58  LEU   B CD1 1 
ATOM   1188 C CD2 . LEU   B 1 59 ? 23.126  -17.733 -34.429 1.00 40.32  ? 58  LEU   B CD2 1 
ATOM   1189 N N   . PHE   B 1 60 ? 19.893  -19.164 -37.723 1.00 34.92  ? 59  PHE   B N   1 
ATOM   1190 C CA  . PHE   B 1 60 ? 19.021  -19.346 -38.873 1.00 35.64  ? 59  PHE   B CA  1 
ATOM   1191 C C   . PHE   B 1 60 ? 18.861  -18.007 -39.587 1.00 41.33  ? 59  PHE   B C   1 
ATOM   1192 O O   . PHE   B 1 60 ? 18.291  -17.054 -39.040 1.00 38.93  ? 59  PHE   B O   1 
ATOM   1193 C CB  . PHE   B 1 60 ? 17.725  -20.054 -38.480 1.00 34.78  ? 59  PHE   B CB  1 
ATOM   1194 C CG  . PHE   B 1 60 ? 17.821  -21.457 -37.883 1.00 36.83  ? 59  PHE   B CG  1 
ATOM   1195 C CD1 . PHE   B 1 60 ? 18.200  -21.652 -36.551 1.00 38.26  ? 59  PHE   B CD1 1 
ATOM   1196 C CD2 . PHE   B 1 60 ? 17.450  -22.575 -38.620 1.00 33.37  ? 59  PHE   B CD2 1 
ATOM   1197 C CE1 . PHE   B 1 60 ? 18.260  -22.929 -36.000 1.00 37.31  ? 59  PHE   B CE1 1 
ATOM   1198 C CE2 . PHE   B 1 60 ? 17.475  -23.848 -38.058 1.00 36.76  ? 59  PHE   B CE2 1 
ATOM   1199 C CZ  . PHE   B 1 60 ? 17.887  -24.028 -36.745 1.00 35.85  ? 59  PHE   B CZ  1 
ATOM   1200 N N   . PRO   B 1 61 ? 19.439  -17.886 -40.809 1.00 44.07  ? 60  PRO   B N   1 
ATOM   1201 C CA  . PRO   B 1 61 ? 19.221  -16.711 -41.658 1.00 45.45  ? 60  PRO   B CA  1 
ATOM   1202 C C   . PRO   B 1 61 ? 17.769  -16.254 -41.595 1.00 45.32  ? 60  PRO   B C   1 
ATOM   1203 O O   . PRO   B 1 61 ? 16.872  -17.012 -41.956 1.00 49.06  ? 60  PRO   B O   1 
ATOM   1204 C CB  . PRO   B 1 61 ? 19.635  -17.290 -43.037 1.00 41.19  ? 60  PRO   B CB  1 
ATOM   1205 C CG  . PRO   B 1 61 ? 20.845  -18.137 -42.706 1.00 41.13  ? 60  PRO   B CG  1 
ATOM   1206 C CD  . PRO   B 1 61 ? 20.429  -18.819 -41.389 1.00 42.56  ? 60  PRO   B CD  1 
ATOM   1207 N N   . TYR   B 1 62 ? 17.571  -15.013 -41.123 1.00 49.99  ? 61  TYR   B N   1 
ATOM   1208 C CA  . TYR   B 1 62 ? 16.283  -14.468 -40.711 1.00 50.54  ? 61  TYR   B CA  1 
ATOM   1209 C C   . TYR   B 1 62 ? 15.252  -14.507 -41.831 1.00 52.28  ? 61  TYR   B C   1 
ATOM   1210 O O   . TYR   B 1 62 ? 14.154  -15.026 -41.628 1.00 51.07  ? 61  TYR   B O   1 
ATOM   1211 C CB  . TYR   B 1 62 ? 16.430  -13.016 -40.265 1.00 46.22  ? 61  TYR   B CB  1 
ATOM   1212 C CG  . TYR   B 1 62 ? 15.117  -12.264 -40.062 1.00 50.20  ? 61  TYR   B CG  1 
ATOM   1213 C CD1 . TYR   B 1 62 ? 14.406  -12.369 -38.869 1.00 48.46  ? 61  TYR   B CD1 1 
ATOM   1214 C CD2 . TYR   B 1 62 ? 14.609  -11.428 -41.049 1.00 49.21  ? 61  TYR   B CD2 1 
ATOM   1215 C CE1 . TYR   B 1 62 ? 13.219  -11.686 -38.674 1.00 49.13  ? 61  TYR   B CE1 1 
ATOM   1216 C CE2 . TYR   B 1 62 ? 13.429  -10.728 -40.863 1.00 53.26  ? 61  TYR   B CE2 1 
ATOM   1217 C CZ  . TYR   B 1 62 ? 12.734  -10.861 -39.674 1.00 51.48  ? 61  TYR   B CZ  1 
ATOM   1218 O OH  . TYR   B 1 62 ? 11.576  -10.176 -39.502 1.00 56.36  ? 61  TYR   B OH  1 
ATOM   1219 N N   . ASP   B 1 63 ? 15.614  -13.908 -42.977 1.00 64.05  ? 62  ASP   B N   1 
ATOM   1220 C CA  . ASP   B 1 63 ? 14.758  -13.777 -44.153 1.00 64.57  ? 62  ASP   B CA  1 
ATOM   1221 C C   . ASP   B 1 63 ? 14.302  -15.151 -44.632 1.00 57.83  ? 62  ASP   B C   1 
ATOM   1222 O O   . ASP   B 1 63 ? 13.148  -15.310 -45.024 1.00 54.01  ? 62  ASP   B O   1 
ATOM   1223 C CB  . ASP   B 1 63 ? 15.409  -12.945 -45.254 1.00 70.08  ? 62  ASP   B CB  1 
ATOM   1224 C CG  . ASP   B 1 63 ? 15.079  -11.452 -45.281 1.00 79.42  ? 62  ASP   B CG  1 
ATOM   1225 O OD1 . ASP   B 1 63 ? 14.133  -11.011 -44.570 1.00 68.39  ? 62  ASP   B OD1 1 
ATOM   1226 O OD2 . ASP   B 1 63 ? 15.774  -10.724 -46.025 1.00 88.35  ? 62  ASP   B OD2 1 
ATOM   1227 N N   . LYS   B 1 64 ? 15.206  -16.140 -44.568 1.00 57.90  ? 63  LYS   B N   1 
ATOM   1228 C CA  . LYS   B 1 64 ? 14.857  -17.518 -44.889 1.00 52.97  ? 63  LYS   B CA  1 
ATOM   1229 C C   . LYS   B 1 64 ? 13.797  -18.053 -43.929 1.00 44.44  ? 63  LYS   B C   1 
ATOM   1230 O O   . LYS   B 1 64 ? 12.913  -18.764 -44.373 1.00 47.80  ? 63  LYS   B O   1 
ATOM   1231 C CB  . LYS   B 1 64 ? 16.030  -18.510 -44.883 1.00 58.10  ? 63  LYS   B CB  1 
ATOM   1232 C CG  . LYS   B 1 64 ? 15.631  -19.945 -45.291 1.00 55.25  ? 63  LYS   B CG  1 
ATOM   1233 C CD  . LYS   B 1 64 ? 16.762  -20.952 -45.428 1.00 57.81  ? 63  LYS   B CD  1 
ATOM   1234 C CE  . LYS   B 1 64 ? 16.417  -22.075 -46.358 1.00 64.34  ? 63  LYS   B CE  1 
ATOM   1235 N NZ  . LYS   B 1 64 ? 15.228  -22.837 -45.979 1.00 59.21  ? 63  LYS   B NZ  1 
ATOM   1236 N N   . SER   B 1 65 ? 13.890  -17.705 -42.636 1.00 44.93  ? 64  SER   B N   1 
ATOM   1237 C CA  . SER   B 1 65 ? 13.187  -18.409 -41.569 1.00 42.32  ? 64  SER   B CA  1 
ATOM   1238 C C   . SER   B 1 65 ? 12.069  -17.605 -40.897 1.00 47.75  ? 64  SER   B C   1 
ATOM   1239 O O   . SER   B 1 65 ? 11.426  -18.134 -39.978 1.00 38.67  ? 64  SER   B O   1 
ATOM   1240 C CB  . SER   B 1 65 ? 14.165  -18.875 -40.547 1.00 45.53  ? 64  SER   B CB  1 
ATOM   1241 O OG  . SER   B 1 65 ? 15.167  -17.891 -40.336 1.00 53.47  ? 64  SER   B OG  1 
ATOM   1242 N N   . LYS   B 1 66 ? 11.834  -16.356 -41.351 1.00 45.51  ? 65  LYS   B N   1 
ATOM   1243 C CA  . LYS   B 1 66 ? 10.898  -15.466 -40.679 1.00 45.51  ? 65  LYS   B CA  1 
ATOM   1244 C C   . LYS   B 1 66 ? 9.516   -16.112 -40.558 1.00 53.53  ? 65  LYS   B C   1 
ATOM   1245 O O   . LYS   B 1 66 ? 8.918   -16.102 -39.484 1.00 49.04  ? 65  LYS   B O   1 
ATOM   1246 C CB  . LYS   B 1 66 ? 10.843  -14.006 -41.161 1.00 48.86  ? 65  LYS   B CB  1 
ATOM   1247 C CG  . LYS   B 1 66 ? 11.229  -13.603 -42.592 1.00 46.75  ? 65  LYS   B CG  1 
ATOM   1248 N N   . ASP   B 1 67 ? 8.995   -16.693 -41.647 1.00 60.98  ? 66  ASP   B N   1 
ATOM   1249 C CA  . ASP   B 1 67 ? 7.631   -17.204 -41.578 1.00 64.13  ? 66  ASP   B CA  1 
ATOM   1250 C C   . ASP   B 1 67 ? 7.514   -18.339 -40.553 1.00 63.37  ? 66  ASP   B C   1 
ATOM   1251 O O   . ASP   B 1 67 ? 6.506   -18.420 -39.847 1.00 65.33  ? 66  ASP   B O   1 
ATOM   1252 C CB  . ASP   B 1 67 ? 6.987   -17.418 -42.942 1.00 73.91  ? 66  ASP   B CB  1 
ATOM   1253 C CG  . ASP   B 1 67 ? 7.771   -18.221 -43.970 1.00 81.05  ? 66  ASP   B CG  1 
ATOM   1254 O OD1 . ASP   B 1 67 ? 7.826   -17.766 -45.138 1.00 82.31  ? 66  ASP   B OD1 1 
ATOM   1255 O OD2 . ASP   B 1 67 ? 8.297   -19.297 -43.605 1.00 81.00  ? 66  ASP   B OD2 1 
ATOM   1256 N N   . LYS   B 1 68 ? 8.552   -19.186 -40.462 1.00 51.65  ? 67  LYS   B N   1 
ATOM   1257 C CA  . LYS   B 1 68 ? 8.550   -20.347 -39.587 1.00 47.58  ? 67  LYS   B CA  1 
ATOM   1258 C C   . LYS   B 1 68 ? 8.666   -19.907 -38.127 1.00 46.45  ? 67  LYS   B C   1 
ATOM   1259 O O   . LYS   B 1 68 ? 7.831   -20.277 -37.314 1.00 43.24  ? 67  LYS   B O   1 
ATOM   1260 C CB  . LYS   B 1 68 ? 9.655   -21.309 -40.045 1.00 51.90  ? 67  LYS   B CB  1 
ATOM   1261 C CG  . LYS   B 1 68 ? 9.682   -22.715 -39.455 1.00 63.06  ? 67  LYS   B CG  1 
ATOM   1262 C CD  . LYS   B 1 68 ? 10.143  -23.798 -40.434 1.00 69.89  ? 67  LYS   B CD  1 
ATOM   1263 C CE  . LYS   B 1 68 ? 10.896  -24.990 -39.879 1.00 76.11  ? 67  LYS   B CE  1 
ATOM   1264 N NZ  . LYS   B 1 68 ? 10.201  -25.793 -38.865 1.00 79.44  ? 67  LYS   B NZ  1 
ATOM   1265 N N   . TYR   B 1 69 ? 9.668   -19.078 -37.800 1.00 48.70  ? 68  TYR   B N   1 
ATOM   1266 C CA  . TYR   B 1 69 ? 9.982   -18.772 -36.403 1.00 47.81  ? 68  TYR   B CA  1 
ATOM   1267 C C   . TYR   B 1 69 ? 9.435   -17.402 -35.976 1.00 44.49  ? 68  TYR   B C   1 
ATOM   1268 O O   . TYR   B 1 69 ? 9.413   -17.058 -34.789 1.00 36.41  ? 68  TYR   B O   1 
ATOM   1269 C CB  . TYR   B 1 69 ? 11.484  -18.933 -36.173 1.00 39.17  ? 68  TYR   B CB  1 
ATOM   1270 C CG  . TYR   B 1 69 ? 12.086  -20.293 -36.527 1.00 47.09  ? 68  TYR   B CG  1 
ATOM   1271 C CD1 . TYR   B 1 69 ? 11.615  -21.476 -35.947 1.00 45.65  ? 68  TYR   B CD1 1 
ATOM   1272 C CD2 . TYR   B 1 69 ? 13.132  -20.394 -37.447 1.00 40.79  ? 68  TYR   B CD2 1 
ATOM   1273 C CE1 . TYR   B 1 69 ? 12.179  -22.704 -36.250 1.00 41.15  ? 68  TYR   B CE1 1 
ATOM   1274 C CE2 . TYR   B 1 69 ? 13.693  -21.618 -37.766 1.00 40.90  ? 68  TYR   B CE2 1 
ATOM   1275 C CZ  . TYR   B 1 69 ? 13.222  -22.768 -37.158 1.00 43.37  ? 68  TYR   B CZ  1 
ATOM   1276 O OH  . TYR   B 1 69 ? 13.790  -23.962 -37.481 1.00 43.55  ? 68  TYR   B OH  1 
ATOM   1277 N N   . GLY   B 1 70 ? 8.935   -16.629 -36.937 1.00 35.00  ? 69  GLY   B N   1 
ATOM   1278 C CA  . GLY   B 1 70 ? 8.596   -15.254 -36.616 1.00 49.64  ? 69  GLY   B CA  1 
ATOM   1279 C C   . GLY   B 1 70 ? 7.255   -15.071 -35.904 1.00 46.83  ? 69  GLY   B C   1 
ATOM   1280 O O   . GLY   B 1 70 ? 6.695   -13.998 -35.978 1.00 49.37  ? 69  GLY   B O   1 
ATOM   1281 N N   . LYS   B 1 71 ? 6.751   -16.092 -35.208 1.00 52.45  ? 70  LYS   B N   1 
ATOM   1282 C CA  . LYS   B 1 71 ? 5.403   -16.036 -34.667 1.00 55.93  ? 70  LYS   B CA  1 
ATOM   1283 C C   . LYS   B 1 71 ? 5.447   -15.543 -33.223 1.00 56.10  ? 70  LYS   B C   1 
ATOM   1284 O O   . LYS   B 1 71 ? 6.308   -15.964 -32.458 1.00 61.12  ? 70  LYS   B O   1 
ATOM   1285 C CB  . LYS   B 1 71 ? 4.710   -17.405 -34.740 1.00 52.39  ? 70  LYS   B CB  1 
ATOM   1286 C CG  . LYS   B 1 71 ? 3.719   -17.595 -35.887 1.00 46.45  ? 70  LYS   B CG  1 
ATOM   1287 C CD  . LYS   B 1 71 ? 4.326   -17.802 -37.261 1.00 42.80  ? 70  LYS   B CD  1 
ATOM   1288 C CE  . LYS   B 1 71 ? 3.275   -17.985 -38.320 1.00 42.19  ? 70  LYS   B CE  1 
ATOM   1289 N NZ  . LYS   B 1 71 ? 3.902   -17.791 -39.635 1.00 40.54  ? 70  LYS   B NZ  1 
ATOM   1290 N N   . PRO   B 1 72 ? 4.517   -14.652 -32.805 1.00 50.39  ? 71  PRO   B N   1 
ATOM   1291 C CA  . PRO   B 1 72 ? 4.443   -14.211 -31.409 1.00 46.39  ? 71  PRO   B CA  1 
ATOM   1292 C C   . PRO   B 1 72 ? 4.292   -15.363 -30.420 1.00 43.62  ? 71  PRO   B C   1 
ATOM   1293 O O   . PRO   B 1 72 ? 3.732   -16.404 -30.750 1.00 52.09  ? 71  PRO   B O   1 
ATOM   1294 C CB  . PRO   B 1 72 ? 3.243   -13.219 -31.341 1.00 47.59  ? 71  PRO   B CB  1 
ATOM   1295 C CG  . PRO   B 1 72 ? 2.913   -12.912 -32.781 1.00 52.74  ? 71  PRO   B CG  1 
ATOM   1296 C CD  . PRO   B 1 72 ? 3.525   -13.995 -33.668 1.00 50.05  ? 71  PRO   B CD  1 
ATOM   1297 N N   . ASN   B 1 73 ? 4.769   -15.157 -29.191 1.00 38.78  ? 72  ASN   B N   1 
ATOM   1298 C CA  . ASN   B 1 73 ? 4.554   -16.127 -28.132 1.00 42.64  ? 72  ASN   B CA  1 
ATOM   1299 C C   . ASN   B 1 73 ? 4.517   -15.396 -26.790 1.00 39.81  ? 72  ASN   B C   1 
ATOM   1300 O O   . ASN   B 1 73 ? 4.520   -14.177 -26.773 1.00 46.34  ? 72  ASN   B O   1 
ATOM   1301 C CB  . ASN   B 1 73 ? 5.488   -17.328 -28.269 1.00 46.93  ? 72  ASN   B CB  1 
ATOM   1302 C CG  . ASN   B 1 73 ? 6.936   -16.951 -28.096 1.00 47.91  ? 72  ASN   B CG  1 
ATOM   1303 O OD1 . ASN   B 1 73 ? 7.245   -16.107 -27.248 1.00 52.11  ? 72  ASN   B OD1 1 
ATOM   1304 N ND2 . ASN   B 1 73 ? 7.829   -17.565 -28.862 1.00 48.00  ? 72  ASN   B ND2 1 
ATOM   1305 N N   . LYS   B 1 74 ? 4.461   -16.142 -25.678 1.00 46.73  ? 73  LYS   B N   1 
ATOM   1306 C CA  . LYS   B 1 74 ? 4.166   -15.614 -24.348 1.00 43.90  ? 73  LYS   B CA  1 
ATOM   1307 C C   . LYS   B 1 74 ? 5.455   -15.485 -23.543 1.00 47.31  ? 73  LYS   B C   1 
ATOM   1308 O O   . LYS   B 1 74 ? 5.431   -15.369 -22.312 1.00 39.34  ? 73  LYS   B O   1 
ATOM   1309 C CB  . LYS   B 1 74 ? 3.251   -16.628 -23.642 1.00 51.26  ? 73  LYS   B CB  1 
ATOM   1310 N N   . ARG   B 1 75 ? 6.584   -15.586 -24.251 1.00 44.86  ? 74  ARG   B N   1 
ATOM   1311 C CA  . ARG   B 1 75 ? 7.882   -15.529 -23.609 1.00 45.38  ? 74  ARG   B CA  1 
ATOM   1312 C C   . ARG   B 1 75 ? 8.303   -14.068 -23.552 1.00 45.70  ? 74  ARG   B C   1 
ATOM   1313 O O   . ARG   B 1 75 ? 8.233   -13.363 -24.570 1.00 37.88  ? 74  ARG   B O   1 
ATOM   1314 C CB  . ARG   B 1 75 ? 8.944   -16.355 -24.343 1.00 47.00  ? 74  ARG   B CB  1 
ATOM   1315 C CG  . ARG   B 1 75 ? 8.633   -17.811 -24.634 1.00 42.12  ? 74  ARG   B CG  1 
ATOM   1316 C CD  . ARG   B 1 75 ? 8.658   -18.567 -23.338 1.00 49.67  ? 74  ARG   B CD  1 
ATOM   1317 N NE  . ARG   B 1 75 ? 8.786   -20.011 -23.567 1.00 48.71  ? 74  ARG   B NE  1 
ATOM   1318 C CZ  . ARG   B 1 75 ? 9.872   -20.711 -23.272 1.00 46.90  ? 74  ARG   B CZ  1 
ATOM   1319 N NH1 . ARG   B 1 75 ? 10.927  -20.115 -22.756 1.00 48.10  ? 74  ARG   B NH1 1 
ATOM   1320 N NH2 . ARG   B 1 75 ? 9.912   -22.011 -23.504 1.00 49.50  ? 74  ARG   B NH2 1 
ATOM   1321 N N   . LYS   B 1 76 ? 8.728   -13.665 -22.342 1.00 39.57  ? 75  LYS   B N   1 
ATOM   1322 C CA  . LYS   B 1 76 ? 9.108   -12.304 -22.008 1.00 39.93  ? 75  LYS   B CA  1 
ATOM   1323 C C   . LYS   B 1 76 ? 10.213  -11.838 -22.942 1.00 35.87  ? 75  LYS   B C   1 
ATOM   1324 O O   . LYS   B 1 76 ? 11.293  -12.429 -22.948 1.00 38.65  ? 75  LYS   B O   1 
ATOM   1325 C CB  . LYS   B 1 76 ? 9.721   -12.239 -20.604 1.00 42.57  ? 75  LYS   B CB  1 
ATOM   1326 C CG  . LYS   B 1 76 ? 10.149  -10.830 -20.232 1.00 49.48  ? 75  LYS   B CG  1 
ATOM   1327 C CD  . LYS   B 1 76 ? 10.780  -10.780 -18.849 1.00 56.18  ? 75  LYS   B CD  1 
ATOM   1328 C CE  . LYS   B 1 76 ? 10.965  -9.388  -18.330 1.00 60.39  ? 75  LYS   B CE  1 
ATOM   1329 N NZ  . LYS   B 1 76 ? 10.967  -9.400  -16.859 1.00 59.55  ? 75  LYS   B NZ  1 
ATOM   1330 N N   . GLY   B 1 77 ? 9.930   -10.764 -23.681 1.00 37.75  ? 76  GLY   B N   1 
ATOM   1331 C CA  . GLY   B 1 77 ? 10.921  -10.078 -24.504 1.00 41.65  ? 76  GLY   B CA  1 
ATOM   1332 C C   . GLY   B 1 77 ? 10.768  -10.433 -25.988 1.00 45.41  ? 76  GLY   B C   1 
ATOM   1333 O O   . GLY   B 1 77 ? 11.323  -9.762  -26.855 1.00 44.66  ? 76  GLY   B O   1 
ATOM   1334 N N   . PHE   B 1 78 ? 9.963   -11.462 -26.270 1.00 39.47  ? 77  PHE   B N   1 
ATOM   1335 C CA  . PHE   B 1 78 ? 9.960   -12.100 -27.577 1.00 40.64  ? 77  PHE   B CA  1 
ATOM   1336 C C   . PHE   B 1 78 ? 9.311   -11.198 -28.616 1.00 35.60  ? 77  PHE   B C   1 
ATOM   1337 O O   . PHE   B 1 78 ? 9.894   -10.953 -29.668 1.00 34.66  ? 77  PHE   B O   1 
ATOM   1338 C CB  . PHE   B 1 78 ? 9.248   -13.453 -27.584 1.00 36.92  ? 77  PHE   B CB  1 
ATOM   1339 C CG  . PHE   B 1 78 ? 9.544   -14.214 -28.866 1.00 41.63  ? 77  PHE   B CG  1 
ATOM   1340 C CD1 . PHE   B 1 78 ? 10.641  -15.079 -28.940 1.00 35.98  ? 77  PHE   B CD1 1 
ATOM   1341 C CD2 . PHE   B 1 78 ? 8.739   -14.046 -29.994 1.00 39.90  ? 77  PHE   B CD2 1 
ATOM   1342 C CE1 . PHE   B 1 78 ? 10.924  -15.774 -30.107 1.00 39.37  ? 77  PHE   B CE1 1 
ATOM   1343 C CE2 . PHE   B 1 78 ? 9.036   -14.735 -31.167 1.00 45.02  ? 77  PHE   B CE2 1 
ATOM   1344 C CZ  . PHE   B 1 78 ? 10.124  -15.606 -31.219 1.00 42.68  ? 77  PHE   B CZ  1 
ATOM   1345 N N   . ASN   B 1 79 ? 8.096   -10.735 -28.304 1.00 37.47  ? 78  ASN   B N   1 
ATOM   1346 C CA  . ASN   B 1 79 ? 7.369   -9.827  -29.175 1.00 38.63  ? 78  ASN   B CA  1 
ATOM   1347 C C   . ASN   B 1 79 ? 8.088   -8.483  -29.307 1.00 36.91  ? 78  ASN   B C   1 
ATOM   1348 O O   . ASN   B 1 79 ? 8.175   -7.945  -30.403 1.00 40.95  ? 78  ASN   B O   1 
ATOM   1349 C CB  . ASN   B 1 79 ? 5.905   -9.690  -28.769 1.00 38.39  ? 78  ASN   B CB  1 
ATOM   1350 C CG  . ASN   B 1 79 ? 5.228   -11.032 -28.662 1.00 38.89  ? 78  ASN   B CG  1 
ATOM   1351 O OD1 . ASN   B 1 79 ? 5.899   -12.065 -28.658 1.00 36.10  ? 78  ASN   B OD1 1 
ATOM   1352 N ND2 . ASN   B 1 79 ? 3.915   -11.036 -28.520 1.00 39.29  ? 78  ASN   B ND2 1 
ATOM   1353 N N   . GLU   B 1 80 ? 8.631   -7.956  -28.215 1.00 36.91  ? 79  GLU   B N   1 
ATOM   1354 C CA  . GLU   B 1 80 ? 9.507   -6.792  -28.324 1.00 47.24  ? 79  GLU   B CA  1 
ATOM   1355 C C   . GLU   B 1 80 ? 10.657  -7.081  -29.285 1.00 45.83  ? 79  GLU   B C   1 
ATOM   1356 O O   . GLU   B 1 80 ? 10.991  -6.218  -30.094 1.00 48.18  ? 79  GLU   B O   1 
ATOM   1357 C CB  . GLU   B 1 80 ? 10.097  -6.306  -26.996 1.00 44.11  ? 79  GLU   B CB  1 
ATOM   1358 C CG  . GLU   B 1 80 ? 9.202   -5.312  -26.253 1.00 59.03  ? 79  GLU   B CG  1 
ATOM   1359 N N   . GLY   B 1 81 ? 11.272  -8.276  -29.149 1.00 45.86  ? 80  GLY   B N   1 
ATOM   1360 C CA  . GLY   B 1 81 ? 12.423  -8.695  -29.935 1.00 38.42  ? 80  GLY   B CA  1 
ATOM   1361 C C   . GLY   B 1 81 ? 12.065  -8.782  -31.418 1.00 41.38  ? 80  GLY   B C   1 
ATOM   1362 O O   . GLY   B 1 81 ? 12.884  -8.484  -32.282 1.00 44.34  ? 80  GLY   B O   1 
ATOM   1363 N N   . LEU   B 1 82 ? 10.829  -9.215  -31.677 1.00 42.51  ? 81  LEU   B N   1 
ATOM   1364 C CA  . LEU   B 1 82 ? 10.240  -9.272  -33.004 1.00 48.92  ? 81  LEU   B CA  1 
ATOM   1365 C C   . LEU   B 1 82 ? 10.083  -7.860  -33.551 1.00 48.84  ? 81  LEU   B C   1 
ATOM   1366 O O   . LEU   B 1 82 ? 10.285  -7.636  -34.741 1.00 56.44  ? 81  LEU   B O   1 
ATOM   1367 C CB  . LEU   B 1 82 ? 8.897   -10.014 -33.007 1.00 42.16  ? 81  LEU   B CB  1 
ATOM   1368 C CG  . LEU   B 1 82 ? 8.973   -11.539 -32.916 1.00 38.37  ? 81  LEU   B CG  1 
ATOM   1369 C CD1 . LEU   B 1 82 ? 7.571   -12.130 -32.999 1.00 33.99  ? 81  LEU   B CD1 1 
ATOM   1370 C CD2 . LEU   B 1 82 ? 9.855   -12.079 -34.029 1.00 35.80  ? 81  LEU   B CD2 1 
ATOM   1371 N N   . TRP   B 1 83 ? 9.701   -6.918  -32.687 1.00 41.34  ? 82  TRP   B N   1 
ATOM   1372 C CA  . TRP   B 1 83 ? 9.594   -5.540  -33.131 1.00 40.99  ? 82  TRP   B CA  1 
ATOM   1373 C C   . TRP   B 1 83 ? 10.959  -5.023  -33.587 1.00 43.27  ? 82  TRP   B C   1 
ATOM   1374 O O   . TRP   B 1 83 ? 11.031  -4.397  -34.649 1.00 44.08  ? 82  TRP   B O   1 
ATOM   1375 C CB  . TRP   B 1 83 ? 8.947   -4.631  -32.071 1.00 40.32  ? 82  TRP   B CB  1 
ATOM   1376 C CG  . TRP   B 1 83 ? 8.765   -3.202  -32.518 1.00 38.93  ? 82  TRP   B CG  1 
ATOM   1377 C CD1 . TRP   B 1 83 ? 7.627   -2.642  -33.018 1.00 42.99  ? 82  TRP   B CD1 1 
ATOM   1378 C CD2 . TRP   B 1 83 ? 9.762   -2.156  -32.545 1.00 41.32  ? 82  TRP   B CD2 1 
ATOM   1379 N NE1 . TRP   B 1 83 ? 7.833   -1.325  -33.331 1.00 44.82  ? 82  TRP   B NE1 1 
ATOM   1380 C CE2 . TRP   B 1 83 ? 9.134   -1.001  -33.063 1.00 42.76  ? 82  TRP   B CE2 1 
ATOM   1381 C CE3 . TRP   B 1 83 ? 11.115  -2.082  -32.179 1.00 42.02  ? 82  TRP   B CE3 1 
ATOM   1382 C CZ2 . TRP   B 1 83 ? 9.810   0.205   -33.225 1.00 47.73  ? 82  TRP   B CZ2 1 
ATOM   1383 C CZ3 . TRP   B 1 83 ? 11.794  -0.894  -32.346 1.00 44.81  ? 82  TRP   B CZ3 1 
ATOM   1384 C CH2 . TRP   B 1 83 ? 11.144  0.233   -32.863 1.00 54.15  ? 82  TRP   B CH2 1 
ATOM   1385 N N   . GLU   B 1 84 ? 12.022  -5.320  -32.811 1.00 36.86  ? 83  GLU   B N   1 
ATOM   1386 C CA  . GLU   B 1 84 ? 13.368  -4.793  -33.044 1.00 36.83  ? 83  GLU   B CA  1 
ATOM   1387 C C   . GLU   B 1 84 ? 13.897  -5.232  -34.398 1.00 37.60  ? 83  GLU   B C   1 
ATOM   1388 O O   . GLU   B 1 84 ? 14.487  -4.446  -35.132 1.00 42.04  ? 83  GLU   B O   1 
ATOM   1389 C CB  . GLU   B 1 84 ? 14.392  -5.133  -31.964 1.00 28.62  ? 83  GLU   B CB  1 
ATOM   1390 C CG  . GLU   B 1 84 ? 13.905  -4.494  -30.674 1.00 31.18  ? 83  GLU   B CG  1 
ATOM   1391 C CD  . GLU   B 1 84 ? 14.646  -4.740  -29.389 1.00 33.70  ? 83  GLU   B CD  1 
ATOM   1392 O OE1 . GLU   B 1 84 ? 15.628  -5.503  -29.364 1.00 33.81  ? 83  GLU   B OE1 1 
ATOM   1393 O OE2 . GLU   B 1 84 ? 14.213  -4.092  -28.411 1.00 37.19  ? 83  GLU   B OE2 1 
ATOM   1394 N N   . ILE   B 1 85 ? 13.640  -6.483  -34.729 1.00 34.50  ? 84  ILE   B N   1 
ATOM   1395 C CA  . ILE   B 1 85 ? 14.330  -7.048  -35.864 1.00 36.39  ? 84  ILE   B CA  1 
ATOM   1396 C C   . ILE   B 1 85 ? 13.613  -6.574  -37.123 1.00 34.41  ? 84  ILE   B C   1 
ATOM   1397 O O   . ILE   B 1 85 ? 14.215  -6.463  -38.185 1.00 29.79  ? 84  ILE   B O   1 
ATOM   1398 C CB  . ILE   B 1 85 ? 14.385  -8.581  -35.710 1.00 37.17  ? 84  ILE   B CB  1 
ATOM   1399 C CG1 . ILE   B 1 85 ? 15.545  -9.186  -36.511 1.00 34.68  ? 84  ILE   B CG1 1 
ATOM   1400 C CG2 . ILE   B 1 85 ? 13.023  -9.206  -36.011 1.00 33.97  ? 84  ILE   B CG2 1 
ATOM   1401 C CD1 . ILE   B 1 85 ? 15.855  -10.643 -36.205 1.00 42.77  ? 84  ILE   B CD1 1 
ATOM   1402 N N   . GLN   B 1 86 ? 12.329  -6.244  -36.966 1.00 40.57  ? 85  GLN   B N   1 
ATOM   1403 C CA  . GLN   B 1 86 ? 11.501  -5.746  -38.058 1.00 43.08  ? 85  GLN   B CA  1 
ATOM   1404 C C   . GLN   B 1 86 ? 11.674  -4.234  -38.272 1.00 44.43  ? 85  GLN   B C   1 
ATOM   1405 O O   . GLN   B 1 86 ? 11.621  -3.746  -39.401 1.00 44.57  ? 85  GLN   B O   1 
ATOM   1406 C CB  . GLN   B 1 86 ? 10.046  -6.145  -37.830 1.00 37.36  ? 85  GLN   B CB  1 
ATOM   1407 N N   . ASN   B 1 87 ? 11.909  -3.469  -37.211 1.00 43.35  ? 86  ASN   B N   1 
ATOM   1408 C CA  . ASN   B 1 87 ? 11.744  -2.026  -37.327 1.00 41.35  ? 86  ASN   B CA  1 
ATOM   1409 C C   . ASN   B 1 87 ? 13.065  -1.266  -37.262 1.00 43.79  ? 86  ASN   B C   1 
ATOM   1410 O O   . ASN   B 1 87 ? 13.163  -0.145  -37.758 1.00 45.25  ? 86  ASN   B O   1 
ATOM   1411 C CB  . ASN   B 1 87 ? 10.770  -1.528  -36.275 1.00 46.94  ? 86  ASN   B CB  1 
ATOM   1412 C CG  . ASN   B 1 87 ? 9.381   -1.932  -36.683 1.00 46.96  ? 86  ASN   B CG  1 
ATOM   1413 O OD1 . ASN   B 1 87 ? 8.709   -1.146  -37.356 1.00 53.32  ? 86  ASN   B OD1 1 
ATOM   1414 N ND2 . ASN   B 1 87 ? 8.985   -3.166  -36.389 1.00 47.40  ? 86  ASN   B ND2 1 
ATOM   1415 N N   . ASN   B 1 88 ? 14.065  -1.873  -36.614 1.00 47.24  ? 87  ASN   B N   1 
ATOM   1416 C CA  . ASN   B 1 88 ? 15.324  -1.201  -36.354 1.00 44.62  ? 87  ASN   B CA  1 
ATOM   1417 C C   . ASN   B 1 88 ? 16.332  -2.234  -35.848 1.00 46.34  ? 87  ASN   B C   1 
ATOM   1418 O O   . ASN   B 1 88 ? 16.819  -2.135  -34.712 1.00 43.90  ? 87  ASN   B O   1 
ATOM   1419 C CB  . ASN   B 1 88 ? 15.130  0.032   -35.465 1.00 44.69  ? 87  ASN   B CB  1 
ATOM   1420 C CG  . ASN   B 1 88 ? 16.349  0.926   -35.481 1.00 44.30  ? 87  ASN   B CG  1 
ATOM   1421 O OD1 . ASN   B 1 88 ? 17.454  0.457   -35.773 1.00 51.52  ? 87  ASN   B OD1 1 
ATOM   1422 N ND2 . ASN   B 1 88 ? 16.182  2.206   -35.186 1.00 43.49  ? 87  ASN   B ND2 1 
ATOM   1423 N N   . PRO   B 1 89 ? 16.668  -3.262  -36.675 1.00 45.05  ? 88  PRO   B N   1 
ATOM   1424 C CA  . PRO   B 1 89 ? 17.697  -4.248  -36.322 1.00 43.53  ? 88  PRO   B CA  1 
ATOM   1425 C C   . PRO   B 1 89 ? 19.100  -3.756  -35.956 1.00 49.87  ? 88  PRO   B C   1 
ATOM   1426 O O   . PRO   B 1 89 ? 19.882  -4.496  -35.354 1.00 53.20  ? 88  PRO   B O   1 
ATOM   1427 C CB  . PRO   B 1 89 ? 17.747  -5.173  -37.573 1.00 42.31  ? 88  PRO   B CB  1 
ATOM   1428 C CG  . PRO   B 1 89 ? 17.120  -4.378  -38.690 1.00 36.32  ? 88  PRO   B CG  1 
ATOM   1429 C CD  . PRO   B 1 89 ? 16.056  -3.550  -37.985 1.00 39.74  ? 88  PRO   B CD  1 
ATOM   1430 N N   . HIS   B 1 90 ? 19.434  -2.516  -36.341 1.00 48.19  ? 89  HIS   B N   1 
ATOM   1431 C CA  . HIS   B 1 90 ? 20.827  -2.101  -36.323 1.00 45.11  ? 89  HIS   B CA  1 
ATOM   1432 C C   . HIS   B 1 90 ? 21.095  -1.075  -35.228 1.00 38.42  ? 89  HIS   B C   1 
ATOM   1433 O O   . HIS   B 1 90 ? 22.170  -0.503  -35.174 1.00 42.27  ? 89  HIS   B O   1 
ATOM   1434 C CB  . HIS   B 1 90 ? 21.275  -1.688  -37.730 1.00 42.73  ? 89  HIS   B CB  1 
ATOM   1435 C CG  . HIS   B 1 90 ? 21.063  -2.779  -38.744 1.00 47.60  ? 89  HIS   B CG  1 
ATOM   1436 N ND1 . HIS   B 1 90 ? 21.723  -3.990  -38.689 1.00 39.43  ? 89  HIS   B ND1 1 
ATOM   1437 C CD2 . HIS   B 1 90 ? 20.236  -2.851  -39.797 1.00 42.04  ? 89  HIS   B CD2 1 
ATOM   1438 C CE1 . HIS   B 1 90 ? 21.333  -4.742  -39.709 1.00 44.07  ? 89  HIS   B CE1 1 
ATOM   1439 N NE2 . HIS   B 1 90 ? 20.440  -4.061  -40.401 1.00 44.02  ? 89  HIS   B NE2 1 
ATOM   1440 N N   . ALA   B 1 91 ? 20.122  -0.853  -34.350 1.00 43.36  ? 90  ALA   B N   1 
ATOM   1441 C CA  . ALA   B 1 91 ? 20.233  0.202   -33.354 1.00 43.65  ? 90  ALA   B CA  1 
ATOM   1442 C C   . ALA   B 1 91 ? 21.164  -0.260  -32.242 1.00 37.59  ? 90  ALA   B C   1 
ATOM   1443 O O   . ALA   B 1 91 ? 21.307  -1.449  -32.035 1.00 40.64  ? 90  ALA   B O   1 
ATOM   1444 C CB  . ALA   B 1 91 ? 18.866  0.519   -32.789 1.00 43.64  ? 90  ALA   B CB  1 
ATOM   1445 N N   . SER   B 1 92 ? 21.780  0.686   -31.536 1.00 43.31  ? 91  SER   B N   1 
ATOM   1446 C CA  . SER   B 1 92 ? 22.334  0.415   -30.218 1.00 47.94  ? 91  SER   B CA  1 
ATOM   1447 C C   . SER   B 1 92 ? 21.197  0.159   -29.226 1.00 45.03  ? 91  SER   B C   1 
ATOM   1448 O O   . SER   B 1 92 ? 20.218  0.912   -29.205 1.00 50.27  ? 91  SER   B O   1 
ATOM   1449 C CB  . SER   B 1 92 ? 23.183  1.559   -29.765 1.00 45.72  ? 91  SER   B CB  1 
ATOM   1450 O OG  . SER   B 1 92 ? 23.743  1.251   -28.497 1.00 56.13  ? 91  SER   B OG  1 
ATOM   1451 N N   . TYR   B 1 93 ? 21.323  -0.908  -28.423 1.00 43.82  ? 92  TYR   B N   1 
ATOM   1452 C CA  . TYR   B 1 93 ? 20.316  -1.229  -27.412 1.00 43.77  ? 92  TYR   B CA  1 
ATOM   1453 C C   . TYR   B 1 93 ? 20.935  -1.182  -26.018 1.00 46.66  ? 92  TYR   B C   1 
ATOM   1454 O O   . TYR   B 1 93 ? 20.393  -1.763  -25.079 1.00 52.50  ? 92  TYR   B O   1 
ATOM   1455 C CB  . TYR   B 1 93 ? 19.578  -2.543  -27.691 1.00 37.50  ? 92  TYR   B CB  1 
ATOM   1456 C CG  . TYR   B 1 93 ? 18.632  -2.447  -28.885 1.00 37.12  ? 92  TYR   B CG  1 
ATOM   1457 C CD1 . TYR   B 1 93 ? 17.345  -1.919  -28.737 1.00 32.43  ? 92  TYR   B CD1 1 
ATOM   1458 C CD2 . TYR   B 1 93 ? 19.031  -2.852  -30.159 1.00 34.76  ? 92  TYR   B CD2 1 
ATOM   1459 C CE1 . TYR   B 1 93 ? 16.468  -1.825  -29.804 1.00 33.16  ? 92  TYR   B CE1 1 
ATOM   1460 C CE2 . TYR   B 1 93 ? 18.156  -2.772  -31.236 1.00 33.23  ? 92  TYR   B CE2 1 
ATOM   1461 C CZ  . TYR   B 1 93 ? 16.885  -2.236  -31.064 1.00 32.21  ? 92  TYR   B CZ  1 
ATOM   1462 O OH  . TYR   B 1 93 ? 16.014  -2.135  -32.108 1.00 26.44  ? 92  TYR   B OH  1 
ATOM   1463 N N   . SER   B 1 94 ? 22.026  -0.423  -25.920 1.00 46.43  ? 93  SER   B N   1 
ATOM   1464 C CA  . SER   B 1 94 ? 22.885  -0.229  -24.758 1.00 60.12  ? 93  SER   B CA  1 
ATOM   1465 C C   . SER   B 1 94 ? 22.121  -0.182  -23.423 1.00 66.24  ? 93  SER   B C   1 
ATOM   1466 O O   . SER   B 1 94 ? 22.659  0.509   -22.511 1.00 65.03  ? 93  SER   B O   1 
ATOM   1467 C CB  . SER   B 1 94 ? 23.685  1.049   -24.907 1.00 54.13  ? 93  SER   B CB  1 
ATOM   1468 O OG  . SER   B 1 94 ? 24.240  1.166   -26.208 1.00 58.25  ? 93  SER   B OG  1 
ATOM   1469 O OXT . SER   B 1 94 ? 21.040  -0.835  -23.316 1.00 70.95  ? 93  SER   B OXT 1 
ATOM   1470 N N   . HIS   C 1 4  ? 32.449  -23.881 26.157  1.00 69.39  ? 3   HIS   C N   1 
ATOM   1471 C CA  . HIS   C 1 4  ? 31.702  -22.718 26.721  1.00 79.80  ? 3   HIS   C CA  1 
ATOM   1472 C C   . HIS   C 1 4  ? 31.307  -23.024 28.170  1.00 84.28  ? 3   HIS   C C   1 
ATOM   1473 O O   . HIS   C 1 4  ? 32.113  -23.545 28.953  1.00 84.37  ? 3   HIS   C O   1 
ATOM   1474 C CB  . HIS   C 1 4  ? 30.517  -22.364 25.806  1.00 71.60  ? 3   HIS   C CB  1 
ATOM   1475 N N   . ALA   C 1 5  ? 30.067  -22.650 28.518  1.00 73.15  ? 4   ALA   C N   1 
ATOM   1476 C CA  . ALA   C 1 5  ? 29.296  -23.275 29.583  1.00 72.50  ? 4   ALA   C CA  1 
ATOM   1477 C C   . ALA   C 1 5  ? 27.824  -22.905 29.416  1.00 81.61  ? 4   ALA   C C   1 
ATOM   1478 O O   . ALA   C 1 5  ? 27.512  -21.902 28.774  1.00 96.87  ? 4   ALA   C O   1 
ATOM   1479 C CB  . ALA   C 1 5  ? 29.832  -22.911 30.938  1.00 70.08  ? 4   ALA   C CB  1 
ATOM   1480 N N   . PHE   C 1 6  ? 26.926  -23.727 29.979  1.00 75.61  ? 5   PHE   C N   1 
ATOM   1481 C CA  . PHE   C 1 6  ? 25.521  -23.641 29.617  1.00 77.08  ? 5   PHE   C CA  1 
ATOM   1482 C C   . PHE   C 1 6  ? 24.637  -23.707 30.859  1.00 84.06  ? 5   PHE   C C   1 
ATOM   1483 O O   . PHE   C 1 6  ? 24.878  -24.528 31.740  1.00 95.55  ? 5   PHE   C O   1 
ATOM   1484 C CB  . PHE   C 1 6  ? 25.167  -24.780 28.653  1.00 68.35  ? 5   PHE   C CB  1 
ATOM   1485 C CG  . PHE   C 1 6  ? 25.989  -24.917 27.376  1.00 64.46  ? 5   PHE   C CG  1 
ATOM   1486 C CD1 . PHE   C 1 6  ? 26.965  -25.900 27.257  1.00 68.23  ? 5   PHE   C CD1 1 
ATOM   1487 C CD2 . PHE   C 1 6  ? 25.777  -24.078 26.286  1.00 71.79  ? 5   PHE   C CD2 1 
ATOM   1488 C CE1 . PHE   C 1 6  ? 27.695  -26.043 26.080  1.00 69.70  ? 5   PHE   C CE1 1 
ATOM   1489 C CE2 . PHE   C 1 6  ? 26.514  -24.213 25.114  1.00 72.75  ? 5   PHE   C CE2 1 
ATOM   1490 C CZ  . PHE   C 1 6  ? 27.470  -25.200 25.010  1.00 70.57  ? 5   PHE   C CZ  1 
ATOM   1491 N N   . LYS   C 1 7  ? 23.600  -22.854 30.894  1.00 83.23  ? 6   LYS   C N   1 
ATOM   1492 C CA  . LYS   C 1 7  ? 22.581  -22.849 31.939  1.00 85.86  ? 6   LYS   C CA  1 
ATOM   1493 C C   . LYS   C 1 7  ? 21.238  -23.262 31.331  1.00 76.23  ? 6   LYS   C C   1 
ATOM   1494 O O   . LYS   C 1 7  ? 21.091  -23.233 30.113  1.00 76.23  ? 6   LYS   C O   1 
ATOM   1495 C CB  . LYS   C 1 7  ? 22.495  -21.465 32.602  1.00 81.01  ? 6   LYS   C CB  1 
ATOM   1496 N N   . PRO   C 1 8  ? 20.220  -23.670 32.132  1.00 78.90  ? 7   PRO   C N   1 
ATOM   1497 C CA  . PRO   C 1 8  ? 18.915  -24.058 31.576  1.00 79.94  ? 7   PRO   C CA  1 
ATOM   1498 C C   . PRO   C 1 8  ? 18.275  -22.960 30.723  1.00 75.26  ? 7   PRO   C C   1 
ATOM   1499 O O   . PRO   C 1 8  ? 18.614  -21.789 30.871  1.00 77.75  ? 7   PRO   C O   1 
ATOM   1500 C CB  . PRO   C 1 8  ? 18.066  -24.432 32.809  1.00 70.57  ? 7   PRO   C CB  1 
ATOM   1501 C CG  . PRO   C 1 8  ? 19.088  -24.734 33.879  1.00 68.62  ? 7   PRO   C CG  1 
ATOM   1502 C CD  . PRO   C 1 8  ? 20.270  -23.814 33.598  1.00 73.57  ? 7   PRO   C CD  1 
ATOM   1503 N N   . GLY   C 1 9  ? 17.386  -23.360 29.801  1.00 74.27  ? 8   GLY   C N   1 
ATOM   1504 C CA  . GLY   C 1 9  ? 16.739  -22.458 28.856  1.00 64.28  ? 8   GLY   C CA  1 
ATOM   1505 C C   . GLY   C 1 9  ? 17.655  -21.987 27.722  1.00 60.61  ? 8   GLY   C C   1 
ATOM   1506 O O   . GLY   C 1 9  ? 17.172  -21.348 26.789  1.00 65.11  ? 8   GLY   C O   1 
ATOM   1507 N N   . ASP   C 1 10 ? 18.962  -22.306 27.797  1.00 53.05  ? 9   ASP   C N   1 
ATOM   1508 C CA  . ASP   C 1 10 ? 19.945  -21.891 26.803  1.00 56.11  ? 9   ASP   C CA  1 
ATOM   1509 C C   . ASP   C 1 10 ? 19.693  -22.576 25.460  1.00 48.26  ? 9   ASP   C C   1 
ATOM   1510 O O   . ASP   C 1 10 ? 19.497  -23.775 25.399  1.00 54.67  ? 9   ASP   C O   1 
ATOM   1511 C CB  . ASP   C 1 10 ? 21.375  -22.080 27.291  1.00 62.53  ? 9   ASP   C CB  1 
ATOM   1512 C CG  . ASP   C 1 10 ? 21.972  -20.944 28.118  1.00 77.05  ? 9   ASP   C CG  1 
ATOM   1513 O OD1 . ASP   C 1 10 ? 21.222  -20.009 28.484  1.00 80.57  ? 9   ASP   C OD1 1 
ATOM   1514 O OD2 . ASP   C 1 10 ? 23.198  -20.989 28.378  1.00 92.49  ? 9   ASP   C OD2 1 
ATOM   1515 N N   . LEU   C 1 11 ? 19.747  -21.800 24.374  1.00 52.70  ? 10  LEU   C N   1 
ATOM   1516 C CA  . LEU   C 1 11 ? 19.375  -22.260 23.046  1.00 44.45  ? 10  LEU   C CA  1 
ATOM   1517 C C   . LEU   C 1 11 ? 20.614  -22.721 22.292  1.00 43.33  ? 10  LEU   C C   1 
ATOM   1518 O O   . LEU   C 1 11 ? 21.592  -21.988 22.196  1.00 47.57  ? 10  LEU   C O   1 
ATOM   1519 C CB  . LEU   C 1 11 ? 18.695  -21.107 22.309  1.00 48.37  ? 10  LEU   C CB  1 
ATOM   1520 C CG  . LEU   C 1 11 ? 17.314  -20.685 22.816  1.00 50.84  ? 10  LEU   C CG  1 
ATOM   1521 C CD1 . LEU   C 1 11 ? 16.590  -19.929 21.719  1.00 48.02  ? 10  LEU   C CD1 1 
ATOM   1522 C CD2 . LEU   C 1 11 ? 16.449  -21.847 23.320  1.00 49.74  ? 10  LEU   C CD2 1 
ATOM   1523 N N   . VAL   C 1 12 ? 20.556  -23.937 21.741  1.00 47.05  ? 11  VAL   C N   1 
ATOM   1524 C CA  . VAL   C 1 12 ? 21.722  -24.561 21.131  1.00 43.97  ? 11  VAL   C CA  1 
ATOM   1525 C C   . VAL   C 1 12 ? 21.312  -25.276 19.840  1.00 46.07  ? 11  VAL   C C   1 
ATOM   1526 O O   . VAL   C 1 12 ? 20.123  -25.456 19.558  1.00 45.41  ? 11  VAL   C O   1 
ATOM   1527 C CB  . VAL   C 1 12 ? 22.331  -25.565 22.129  1.00 39.97  ? 11  VAL   C CB  1 
ATOM   1528 C CG1 . VAL   C 1 12 ? 22.950  -24.892 23.339  1.00 40.26  ? 11  VAL   C CG1 1 
ATOM   1529 C CG2 . VAL   C 1 12 ? 21.299  -26.574 22.602  1.00 43.96  ? 11  VAL   C CG2 1 
ATOM   1530 N N   . PHE   C 1 13 ? 22.317  -25.647 19.040  1.00 38.40  ? 12  PHE   C N   1 
ATOM   1531 C CA  . PHE   C 1 13 ? 22.211  -26.805 18.180  1.00 40.56  ? 12  PHE   C CA  1 
ATOM   1532 C C   . PHE   C 1 13 ? 22.904  -27.947 18.891  1.00 41.98  ? 12  PHE   C C   1 
ATOM   1533 O O   . PHE   C 1 13 ? 24.037  -27.802 19.366  1.00 39.33  ? 12  PHE   C O   1 
ATOM   1534 C CB  . PHE   C 1 13 ? 22.857  -26.684 16.799  1.00 44.62  ? 12  PHE   C CB  1 
ATOM   1535 C CG  . PHE   C 1 13 ? 22.116  -25.668 15.955  1.00 44.48  ? 12  PHE   C CG  1 
ATOM   1536 C CD1 . PHE   C 1 13 ? 21.112  -26.072 15.087  1.00 43.88  ? 12  PHE   C CD1 1 
ATOM   1537 C CD2 . PHE   C 1 13 ? 22.412  -24.309 16.053  1.00 50.43  ? 12  PHE   C CD2 1 
ATOM   1538 C CE1 . PHE   C 1 13 ? 20.443  -25.140 14.320  1.00 45.53  ? 12  PHE   C CE1 1 
ATOM   1539 C CE2 . PHE   C 1 13 ? 21.726  -23.373 15.288  1.00 47.32  ? 12  PHE   C CE2 1 
ATOM   1540 C CZ  . PHE   C 1 13 ? 20.743  -23.796 14.429  1.00 49.51  ? 12  PHE   C CZ  1 
ATOM   1541 N N   . ALA   C 1 14 ? 22.164  -29.056 18.971  1.00 41.62  ? 13  ALA   C N   1 
ATOM   1542 C CA  . ALA   C 1 14 ? 22.611  -30.268 19.622  1.00 39.57  ? 13  ALA   C CA  1 
ATOM   1543 C C   . ALA   C 1 14 ? 22.950  -31.258 18.526  1.00 42.07  ? 13  ALA   C C   1 
ATOM   1544 O O   . ALA   C 1 14 ? 22.264  -31.322 17.508  1.00 46.00  ? 13  ALA   C O   1 
ATOM   1545 C CB  . ALA   C 1 14 ? 21.519  -30.802 20.524  1.00 33.42  ? 13  ALA   C CB  1 
ATOM   1546 N N   . LYS   C 1 15 ? 24.046  -31.978 18.729  1.00 39.74  ? 14  LYS   C N   1 
ATOM   1547 C CA  . LYS   C 1 15 ? 24.450  -32.986 17.776  1.00 41.83  ? 14  LYS   C CA  1 
ATOM   1548 C C   . LYS   C 1 15 ? 24.463  -34.308 18.506  1.00 41.38  ? 14  LYS   C C   1 
ATOM   1549 O O   . LYS   C 1 15 ? 25.087  -34.394 19.552  1.00 47.39  ? 14  LYS   C O   1 
ATOM   1550 C CB  . LYS   C 1 15 ? 25.900  -32.827 17.321  1.00 42.89  ? 14  LYS   C CB  1 
ATOM   1551 C CG  . LYS   C 1 15 ? 26.258  -33.794 16.209  1.00 42.92  ? 14  LYS   C CG  1 
ATOM   1552 C CD  . LYS   C 1 15 ? 25.388  -33.674 14.960  1.00 43.91  ? 14  LYS   C CD  1 
ATOM   1553 C CE  . LYS   C 1 15 ? 26.003  -34.504 13.869  1.00 46.70  ? 14  LYS   C CE  1 
ATOM   1554 N NZ  . LYS   C 1 15 ? 25.970  -35.940 14.201  1.00 45.12  ? 14  LYS   C NZ  1 
ATOM   1555 N N   . MET   C 1 16 ? 23.731  -35.277 17.952  1.00 44.99  ? 15  MET   C N   1 
ATOM   1556 C CA  . MET   C 1 16 ? 23.827  -36.675 18.307  1.00 42.87  ? 15  MET   C CA  1 
ATOM   1557 C C   . MET   C 1 16 ? 24.289  -37.425 17.066  1.00 49.61  ? 15  MET   C C   1 
ATOM   1558 O O   . MET   C 1 16 ? 24.181  -36.908 15.953  1.00 49.74  ? 15  MET   C O   1 
ATOM   1559 C CB  . MET   C 1 16 ? 22.444  -37.225 18.643  1.00 42.82  ? 15  MET   C CB  1 
ATOM   1560 C CG  . MET   C 1 16 ? 21.801  -36.551 19.820  1.00 49.86  ? 15  MET   C CG  1 
ATOM   1561 S SD  . MET   C 1 16 ? 20.284  -37.373 20.345  1.00 56.46  ? 15  MET   C SD  1 
ATOM   1562 C CE  . MET   C 1 16 ? 19.300  -37.143 18.851  1.00 52.41  ? 15  MET   C CE  1 
ATOM   1563 N N   . LYS   C 1 17 ? 24.758  -38.660 17.276  1.00 53.36  ? 16  LYS   C N   1 
ATOM   1564 C CA  . LYS   C 1 17 ? 25.198  -39.540 16.202  1.00 56.06  ? 16  LYS   C CA  1 
ATOM   1565 C C   . LYS   C 1 17 ? 23.976  -39.960 15.380  1.00 48.07  ? 16  LYS   C C   1 
ATOM   1566 O O   . LYS   C 1 17 ? 22.936  -40.313 15.932  1.00 42.37  ? 16  LYS   C O   1 
ATOM   1567 C CB  . LYS   C 1 17 ? 25.979  -40.729 16.793  1.00 52.36  ? 16  LYS   C CB  1 
ATOM   1568 C CG  . LYS   C 1 17 ? 26.765  -41.589 15.820  1.00 49.71  ? 16  LYS   C CG  1 
ATOM   1569 C CD  . LYS   C 1 17 ? 28.030  -40.947 15.264  1.00 50.27  ? 16  LYS   C CD  1 
ATOM   1570 C CE  . LYS   C 1 17 ? 28.319  -41.509 13.916  1.00 54.16  ? 16  LYS   C CE  1 
ATOM   1571 N NZ  . LYS   C 1 17 ? 29.657  -41.181 13.420  1.00 60.03  ? 16  LYS   C NZ  1 
ATOM   1572 N N   . GLY   C 1 18 ? 24.123  -39.904 14.052  1.00 47.69  ? 17  GLY   C N   1 
ATOM   1573 C CA  . GLY   C 1 18 ? 23.107  -40.391 13.136  1.00 44.62  ? 17  GLY   C CA  1 
ATOM   1574 C C   . GLY   C 1 18 ? 22.073  -39.304 12.859  1.00 45.29  ? 17  GLY   C C   1 
ATOM   1575 O O   . GLY   C 1 18 ? 21.017  -39.560 12.292  1.00 43.82  ? 17  GLY   C O   1 
ATOM   1576 N N   . TYR   C 1 19 ? 22.394  -38.083 13.278  1.00 49.47  ? 18  TYR   C N   1 
ATOM   1577 C CA  . TYR   C 1 19 ? 21.441  -36.986 13.267  1.00 51.37  ? 18  TYR   C CA  1 
ATOM   1578 C C   . TYR   C 1 19 ? 22.212  -35.712 12.959  1.00 50.84  ? 18  TYR   C C   1 
ATOM   1579 O O   . TYR   C 1 19 ? 23.341  -35.534 13.414  1.00 51.15  ? 18  TYR   C O   1 
ATOM   1580 C CB  . TYR   C 1 19 ? 20.690  -36.804 14.595  1.00 46.16  ? 18  TYR   C CB  1 
ATOM   1581 C CG  . TYR   C 1 19 ? 19.706  -37.914 14.928  1.00 44.40  ? 18  TYR   C CG  1 
ATOM   1582 C CD1 . TYR   C 1 19 ? 20.098  -39.067 15.604  1.00 42.02  ? 18  TYR   C CD1 1 
ATOM   1583 C CD2 . TYR   C 1 19 ? 18.379  -37.806 14.536  1.00 50.30  ? 18  TYR   C CD2 1 
ATOM   1584 C CE1 . TYR   C 1 19 ? 19.184  -40.069 15.904  1.00 43.19  ? 18  TYR   C CE1 1 
ATOM   1585 C CE2 . TYR   C 1 19 ? 17.462  -38.807 14.808  1.00 52.12  ? 18  TYR   C CE2 1 
ATOM   1586 C CZ  . TYR   C 1 19 ? 17.864  -39.931 15.501  1.00 47.77  ? 18  TYR   C CZ  1 
ATOM   1587 O OH  . TYR   C 1 19 ? 16.909  -40.871 15.733  1.00 51.14  ? 18  TYR   C OH  1 
ATOM   1588 N N   . PRO   C 1 20 ? 21.622  -34.801 12.164  1.00 45.76  ? 19  PRO   C N   1 
ATOM   1589 C CA  . PRO   C 1 20 ? 22.275  -33.533 11.879  1.00 45.28  ? 19  PRO   C CA  1 
ATOM   1590 C C   . PRO   C 1 20 ? 22.145  -32.741 13.177  1.00 49.27  ? 19  PRO   C C   1 
ATOM   1591 O O   . PRO   C 1 20 ? 21.420  -33.173 14.089  1.00 41.32  ? 19  PRO   C O   1 
ATOM   1592 C CB  . PRO   C 1 20 ? 21.405  -33.021 10.727  1.00 40.33  ? 19  PRO   C CB  1 
ATOM   1593 C CG  . PRO   C 1 20 ? 20.017  -33.523 11.060  1.00 44.05  ? 19  PRO   C CG  1 
ATOM   1594 C CD  . PRO   C 1 20 ? 20.314  -34.948 11.502  1.00 47.38  ? 19  PRO   C CD  1 
ATOM   1595 N N   . HIS   C 1 21 ? 22.899  -31.628 13.241  1.00 48.30  ? 20  HIS   C N   1 
ATOM   1596 C CA  . HIS   C 1 21 ? 22.846  -30.651 14.314  1.00 47.52  ? 20  HIS   C CA  1 
ATOM   1597 C C   . HIS   C 1 21 ? 21.417  -30.141 14.414  1.00 45.49  ? 20  HIS   C C   1 
ATOM   1598 O O   . HIS   C 1 21 ? 20.863  -29.681 13.416  1.00 43.85  ? 20  HIS   C O   1 
ATOM   1599 C CB  . HIS   C 1 21 ? 23.816  -29.508 14.012  1.00 53.24  ? 20  HIS   C CB  1 
ATOM   1600 C CG  . HIS   C 1 21 ? 25.248  -29.920 14.081  1.00 57.32  ? 20  HIS   C CG  1 
ATOM   1601 N ND1 . HIS   C 1 21 ? 25.952  -30.383 12.990  1.00 57.58  ? 20  HIS   C ND1 1 
ATOM   1602 C CD2 . HIS   C 1 21 ? 26.106  -29.948 15.122  1.00 57.48  ? 20  HIS   C CD2 1 
ATOM   1603 C CE1 . HIS   C 1 21 ? 27.196  -30.659 13.367  1.00 62.83  ? 20  HIS   C CE1 1 
ATOM   1604 N NE2 . HIS   C 1 21 ? 27.313  -30.400 14.657  1.00 60.04  ? 20  HIS   C NE2 1 
ATOM   1605 N N   . TRP   C 1 22 ? 20.835  -30.280 15.610  1.00 42.40  ? 21  TRP   C N   1 
ATOM   1606 C CA  . TRP   C 1 22 ? 19.399  -30.164 15.810  1.00 43.90  ? 21  TRP   C CA  1 
ATOM   1607 C C   . TRP   C 1 22 ? 19.111  -28.988 16.725  1.00 42.61  ? 21  TRP   C C   1 
ATOM   1608 O O   . TRP   C 1 22 ? 19.707  -28.901 17.797  1.00 50.24  ? 21  TRP   C O   1 
ATOM   1609 C CB  . TRP   C 1 22 ? 18.823  -31.432 16.461  1.00 47.03  ? 21  TRP   C CB  1 
ATOM   1610 C CG  . TRP   C 1 22 ? 17.371  -31.671 16.126  1.00 48.37  ? 21  TRP   C CG  1 
ATOM   1611 C CD1 . TRP   C 1 22 ? 16.254  -31.126 16.701  1.00 46.19  ? 21  TRP   C CD1 1 
ATOM   1612 C CD2 . TRP   C 1 22 ? 16.895  -32.554 15.084  1.00 46.23  ? 21  TRP   C CD2 1 
ATOM   1613 N NE1 . TRP   C 1 22 ? 15.120  -31.589 16.084  1.00 39.65  ? 21  TRP   C NE1 1 
ATOM   1614 C CE2 . TRP   C 1 22 ? 15.482  -32.465 15.089  1.00 47.22  ? 21  TRP   C CE2 1 
ATOM   1615 C CE3 . TRP   C 1 22 ? 17.530  -33.380 14.146  1.00 40.64  ? 21  TRP   C CE3 1 
ATOM   1616 C CZ2 . TRP   C 1 22 ? 14.704  -33.200 14.196  1.00 49.13  ? 21  TRP   C CZ2 1 
ATOM   1617 C CZ3 . TRP   C 1 22 ? 16.758  -34.095 13.258  1.00 42.42  ? 21  TRP   C CZ3 1 
ATOM   1618 C CH2 . TRP   C 1 22 ? 15.367  -34.026 13.308  1.00 48.00  ? 21  TRP   C CH2 1 
ATOM   1619 N N   . PRO   C 1 23 ? 18.154  -28.106 16.351  1.00 39.71  ? 22  PRO   C N   1 
ATOM   1620 C CA  . PRO   C 1 23 ? 17.774  -26.968 17.181  1.00 39.05  ? 22  PRO   C CA  1 
ATOM   1621 C C   . PRO   C 1 23 ? 17.209  -27.500 18.495  1.00 35.68  ? 22  PRO   C C   1 
ATOM   1622 O O   . PRO   C 1 23 ? 16.377  -28.406 18.482  1.00 37.15  ? 22  PRO   C O   1 
ATOM   1623 C CB  . PRO   C 1 23 ? 16.696  -26.330 16.275  1.00 42.27  ? 22  PRO   C CB  1 
ATOM   1624 C CG  . PRO   C 1 23 ? 16.098  -27.523 15.554  1.00 36.80  ? 22  PRO   C CG  1 
ATOM   1625 C CD  . PRO   C 1 23 ? 17.391  -28.157 15.092  1.00 40.83  ? 22  PRO   C CD  1 
ATOM   1626 N N   . ALA   C 1 24 ? 17.664  -26.936 19.617  1.00 32.18  ? 23  ALA   C N   1 
ATOM   1627 C CA  . ALA   C 1 24 ? 17.443  -27.585 20.902  1.00 32.36  ? 23  ALA   C CA  1 
ATOM   1628 C C   . ALA   C 1 24 ? 17.705  -26.575 22.005  1.00 35.41  ? 23  ALA   C C   1 
ATOM   1629 O O   . ALA   C 1 24 ? 18.143  -25.471 21.720  1.00 37.87  ? 23  ALA   C O   1 
ATOM   1630 C CB  . ALA   C 1 24 ? 18.378  -28.781 21.018  1.00 34.67  ? 23  ALA   C CB  1 
ATOM   1631 N N   . ARG   C 1 25 ? 17.456  -26.957 23.267  1.00 38.54  ? 24  ARG   C N   1 
ATOM   1632 C CA  . ARG   C 1 25 ? 17.711  -26.033 24.356  1.00 36.72  ? 24  ARG   C CA  1 
ATOM   1633 C C   . ARG   C 1 25 ? 18.040  -26.817 25.621  1.00 42.88  ? 24  ARG   C C   1 
ATOM   1634 O O   . ARG   C 1 25 ? 17.614  -27.957 25.779  1.00 42.46  ? 24  ARG   C O   1 
ATOM   1635 C CB  . ARG   C 1 25 ? 16.462  -25.184 24.614  1.00 48.52  ? 24  ARG   C CB  1 
ATOM   1636 C CG  . ARG   C 1 25 ? 15.254  -25.888 25.220  1.00 50.21  ? 24  ARG   C CG  1 
ATOM   1637 C CD  . ARG   C 1 25 ? 14.095  -24.985 25.608  1.00 52.05  ? 24  ARG   C CD  1 
ATOM   1638 N NE  . ARG   C 1 25 ? 13.016  -25.796 26.195  1.00 64.77  ? 24  ARG   C NE  1 
ATOM   1639 C CZ  . ARG   C 1 25 ? 11.715  -25.508 26.287  1.00 61.95  ? 24  ARG   C CZ  1 
ATOM   1640 N NH1 . ARG   C 1 25 ? 11.235  -24.388 25.773  1.00 60.36  ? 24  ARG   C NH1 1 
ATOM   1641 N NH2 . ARG   C 1 25 ? 10.889  -26.365 26.867  1.00 58.02  ? 24  ARG   C NH2 1 
ATOM   1642 N N   . ILE   C 1 26 ? 18.770  -26.169 26.532  1.00 52.30  ? 25  ILE   C N   1 
ATOM   1643 C CA  . ILE   C 1 26 ? 19.096  -26.756 27.819  1.00 60.84  ? 25  ILE   C CA  1 
ATOM   1644 C C   . ILE   C 1 26 ? 17.852  -26.732 28.696  1.00 67.31  ? 25  ILE   C C   1 
ATOM   1645 O O   . ILE   C 1 26 ? 17.269  -25.676 28.926  1.00 75.50  ? 25  ILE   C O   1 
ATOM   1646 C CB  . ILE   C 1 26 ? 20.275  -26.032 28.499  1.00 59.74  ? 25  ILE   C CB  1 
ATOM   1647 C CG1 . ILE   C 1 26 ? 21.340  -25.624 27.496  1.00 57.64  ? 25  ILE   C CG1 1 
ATOM   1648 C CG2 . ILE   C 1 26 ? 20.866  -26.901 29.613  1.00 57.62  ? 25  ILE   C CG2 1 
ATOM   1649 C CD1 . ILE   C 1 26 ? 22.009  -26.805 26.820  1.00 58.37  ? 25  ILE   C CD1 1 
ATOM   1650 N N   . ASP   C 1 27 ? 17.462  -27.917 29.171  1.00 71.67  ? 26  ASP   C N   1 
ATOM   1651 C CA  . ASP   C 1 27 ? 16.490  -28.041 30.243  1.00 84.36  ? 26  ASP   C CA  1 
ATOM   1652 C C   . ASP   C 1 27 ? 17.154  -27.725 31.585  1.00 90.33  ? 26  ASP   C C   1 
ATOM   1653 O O   . ASP   C 1 27 ? 18.375  -27.638 31.674  1.00 102.42 ? 26  ASP   C O   1 
ATOM   1654 C CB  . ASP   C 1 27 ? 15.863  -29.430 30.264  1.00 86.33  ? 26  ASP   C CB  1 
ATOM   1655 C CG  . ASP   C 1 27 ? 14.694  -29.655 29.313  1.00 83.14  ? 26  ASP   C CG  1 
ATOM   1656 O OD1 . ASP   C 1 27 ? 14.437  -28.744 28.499  1.00 80.65  ? 26  ASP   C OD1 1 
ATOM   1657 O OD2 . ASP   C 1 27 ? 14.033  -30.723 29.414  1.00 76.98  ? 26  ASP   C OD2 1 
ATOM   1658 N N   . ASP   C 1 28 ? 16.330  -27.541 32.624  1.00 95.42  ? 27  ASP   C N   1 
ATOM   1659 C CA  . ASP   C 1 28 ? 16.774  -27.725 33.996  1.00 91.77  ? 27  ASP   C CA  1 
ATOM   1660 C C   . ASP   C 1 28 ? 16.569  -29.195 34.362  1.00 82.95  ? 27  ASP   C C   1 
ATOM   1661 O O   . ASP   C 1 28 ? 15.755  -29.878 33.745  1.00 73.78  ? 27  ASP   C O   1 
ATOM   1662 C CB  . ASP   C 1 28 ? 16.100  -26.745 34.946  1.00 94.02  ? 27  ASP   C CB  1 
ATOM   1663 N N   . ILE   C 1 29 ? 17.328  -29.676 35.352  1.00 77.70  ? 28  ILE   C N   1 
ATOM   1664 C CA  . ILE   C 1 29 ? 17.182  -31.042 35.823  1.00 88.00  ? 28  ILE   C CA  1 
ATOM   1665 C C   . ILE   C 1 29 ? 16.325  -31.025 37.088  1.00 97.73  ? 28  ILE   C C   1 
ATOM   1666 O O   . ILE   C 1 29 ? 16.451  -30.117 37.907  1.00 99.11  ? 28  ILE   C O   1 
ATOM   1667 C CB  . ILE   C 1 29 ? 18.559  -31.695 36.054  1.00 89.48  ? 28  ILE   C CB  1 
ATOM   1668 N N   . ALA   C 1 30 ? 15.456  -32.037 37.231  1.00 100.22 ? 29  ALA   C N   1 
ATOM   1669 C CA  . ALA   C 1 30 ? 14.540  -32.143 38.357  1.00 97.28  ? 29  ALA   C CA  1 
ATOM   1670 C C   . ALA   C 1 30 ? 15.306  -32.493 39.641  1.00 98.23  ? 29  ALA   C C   1 
ATOM   1671 O O   . ALA   C 1 30 ? 15.155  -33.624 40.173  1.00 106.66 ? 29  ALA   C O   1 
ATOM   1672 C CB  . ALA   C 1 30 ? 13.448  -33.145 38.041  1.00 104.76 ? 29  ALA   C CB  1 
ATOM   1673 N N   . LYS   C 1 35 ? 19.408  -38.254 38.051  1.00 91.66  ? 34  LYS   C N   1 
ATOM   1674 C CA  . LYS   C 1 35 ? 20.478  -37.257 37.773  1.00 80.07  ? 34  LYS   C CA  1 
ATOM   1675 C C   . LYS   C 1 35 ? 21.062  -37.544 36.388  1.00 79.08  ? 34  LYS   C C   1 
ATOM   1676 O O   . LYS   C 1 35 ? 20.926  -38.660 35.884  1.00 81.99  ? 34  LYS   C O   1 
ATOM   1677 C CB  . LYS   C 1 35 ? 21.485  -37.223 38.933  1.00 61.20  ? 34  LYS   C CB  1 
ATOM   1678 N N   . PRO   C 1 36 ? 21.692  -36.543 35.722  1.00 80.16  ? 35  PRO   C N   1 
ATOM   1679 C CA  . PRO   C 1 36 ? 22.312  -36.749 34.410  1.00 74.72  ? 35  PRO   C CA  1 
ATOM   1680 C C   . PRO   C 1 36 ? 23.566  -37.606 34.565  1.00 82.51  ? 35  PRO   C C   1 
ATOM   1681 O O   . PRO   C 1 36 ? 24.106  -37.720 35.667  1.00 89.15  ? 35  PRO   C O   1 
ATOM   1682 C CB  . PRO   C 1 36 ? 22.670  -35.316 33.942  1.00 78.88  ? 35  PRO   C CB  1 
ATOM   1683 C CG  . PRO   C 1 36 ? 21.991  -34.372 34.916  1.00 80.52  ? 35  PRO   C CG  1 
ATOM   1684 C CD  . PRO   C 1 36 ? 21.843  -35.160 36.206  1.00 87.08  ? 35  PRO   C CD  1 
ATOM   1685 N N   . PRO   C 1 37 ? 24.102  -38.216 33.482  1.00 73.15  ? 36  PRO   C N   1 
ATOM   1686 C CA  . PRO   C 1 37 ? 25.418  -38.849 33.554  1.00 69.92  ? 36  PRO   C CA  1 
ATOM   1687 C C   . PRO   C 1 37 ? 26.464  -37.755 33.786  1.00 72.03  ? 36  PRO   C C   1 
ATOM   1688 O O   . PRO   C 1 37 ? 26.217  -36.579 33.489  1.00 64.51  ? 36  PRO   C O   1 
ATOM   1689 C CB  . PRO   C 1 37 ? 25.554  -39.552 32.187  1.00 65.92  ? 36  PRO   C CB  1 
ATOM   1690 C CG  . PRO   C 1 37 ? 24.140  -39.618 31.665  1.00 65.03  ? 36  PRO   C CG  1 
ATOM   1691 C CD  . PRO   C 1 37 ? 23.495  -38.329 32.148  1.00 68.34  ? 36  PRO   C CD  1 
ATOM   1692 N N   . PRO   C 1 38 ? 27.660  -38.088 34.335  1.00 66.72  ? 37  PRO   C N   1 
ATOM   1693 C CA  . PRO   C 1 38 ? 28.643  -37.069 34.694  1.00 63.25  ? 37  PRO   C CA  1 
ATOM   1694 C C   . PRO   C 1 38 ? 28.893  -36.174 33.490  1.00 63.85  ? 37  PRO   C C   1 
ATOM   1695 O O   . PRO   C 1 38 ? 29.281  -36.651 32.420  1.00 60.82  ? 37  PRO   C O   1 
ATOM   1696 C CB  . PRO   C 1 38 ? 29.895  -37.857 35.116  1.00 64.74  ? 37  PRO   C CB  1 
ATOM   1697 C CG  . PRO   C 1 38 ? 29.352  -39.216 35.513  1.00 64.76  ? 37  PRO   C CG  1 
ATOM   1698 C CD  . PRO   C 1 38 ? 28.144  -39.450 34.615  1.00 65.23  ? 37  PRO   C CD  1 
ATOM   1699 N N   . ASN   C 1 39 ? 28.586  -34.888 33.689  1.00 69.68  ? 38  ASN   C N   1 
ATOM   1700 C CA  . ASN   C 1 39 ? 28.970  -33.803 32.801  1.00 71.35  ? 38  ASN   C CA  1 
ATOM   1701 C C   . ASN   C 1 39 ? 28.205  -33.863 31.472  1.00 71.21  ? 38  ASN   C C   1 
ATOM   1702 O O   . ASN   C 1 39 ? 28.689  -33.362 30.452  1.00 64.73  ? 38  ASN   C O   1 
ATOM   1703 C CB  . ASN   C 1 39 ? 30.485  -33.654 32.700  1.00 66.00  ? 38  ASN   C CB  1 
ATOM   1704 C CG  . ASN   C 1 39 ? 30.841  -32.447 31.870  1.00 77.15  ? 38  ASN   C CG  1 
ATOM   1705 O OD1 . ASN   C 1 39 ? 30.518  -31.312 32.245  1.00 65.04  ? 38  ASN   C OD1 1 
ATOM   1706 N ND2 . ASN   C 1 39 ? 31.452  -32.678 30.717  1.00 83.23  ? 38  ASN   C ND2 1 
ATOM   1707 N N   . LYS   C 1 40 ? 26.997  -34.450 31.509  1.00 59.47  ? 39  LYS   C N   1 
ATOM   1708 C CA  . LYS   C 1 40 ? 26.054  -34.371 30.404  1.00 58.59  ? 39  LYS   C CA  1 
ATOM   1709 C C   . LYS   C 1 40 ? 24.936  -33.423 30.818  1.00 54.87  ? 39  LYS   C C   1 
ATOM   1710 O O   . LYS   C 1 40 ? 24.593  -33.366 31.999  1.00 61.75  ? 39  LYS   C O   1 
ATOM   1711 C CB  . LYS   C 1 40 ? 25.480  -35.754 30.079  1.00 60.17  ? 39  LYS   C CB  1 
ATOM   1712 C CG  . LYS   C 1 40 ? 26.508  -36.852 29.875  1.00 61.96  ? 39  LYS   C CG  1 
ATOM   1713 C CD  . LYS   C 1 40 ? 27.326  -36.684 28.606  1.00 61.49  ? 39  LYS   C CD  1 
ATOM   1714 C CE  . LYS   C 1 40 ? 28.260  -37.837 28.426  1.00 64.02  ? 39  LYS   C CE  1 
ATOM   1715 N NZ  . LYS   C 1 40 ? 29.313  -37.480 27.465  1.00 70.26  ? 39  LYS   C NZ  1 
ATOM   1716 N N   . TYR   C 1 41 ? 24.406  -32.661 29.851  1.00 56.88  ? 40  TYR   C N   1 
ATOM   1717 C CA  . TYR   C 1 41 ? 23.309  -31.720 30.079  1.00 51.55  ? 40  TYR   C CA  1 
ATOM   1718 C C   . TYR   C 1 41 ? 21.992  -32.332 29.580  1.00 56.42  ? 40  TYR   C C   1 
ATOM   1719 O O   . TYR   C 1 41 ? 21.966  -33.100 28.612  1.00 59.31  ? 40  TYR   C O   1 
ATOM   1720 C CB  . TYR   C 1 41 ? 23.544  -30.405 29.327  1.00 53.15  ? 40  TYR   C CB  1 
ATOM   1721 C CG  . TYR   C 1 41 ? 24.739  -29.526 29.687  1.00 58.13  ? 40  TYR   C CG  1 
ATOM   1722 C CD1 . TYR   C 1 41 ? 26.040  -29.861 29.314  1.00 61.66  ? 40  TYR   C CD1 1 
ATOM   1723 C CD2 . TYR   C 1 41 ? 24.551  -28.311 30.334  1.00 58.22  ? 40  TYR   C CD2 1 
ATOM   1724 C CE1 . TYR   C 1 41 ? 27.116  -29.042 29.625  1.00 63.48  ? 40  TYR   C CE1 1 
ATOM   1725 C CE2 . TYR   C 1 41 ? 25.615  -27.479 30.642  1.00 62.20  ? 40  TYR   C CE2 1 
ATOM   1726 C CZ  . TYR   C 1 41 ? 26.898  -27.842 30.283  1.00 61.73  ? 40  TYR   C CZ  1 
ATOM   1727 O OH  . TYR   C 1 41 ? 27.912  -26.991 30.591  1.00 59.43  ? 40  TYR   C OH  1 
ATOM   1728 N N   . PRO   C 1 42 ? 20.835  -32.017 30.208  1.00 55.83  ? 41  PRO   C N   1 
ATOM   1729 C CA  . PRO   C 1 42 ? 19.544  -32.431 29.657  1.00 49.87  ? 41  PRO   C CA  1 
ATOM   1730 C C   . PRO   C 1 42 ? 19.200  -31.543 28.467  1.00 46.80  ? 41  PRO   C C   1 
ATOM   1731 O O   . PRO   C 1 42 ? 19.278  -30.325 28.590  1.00 53.67  ? 41  PRO   C O   1 
ATOM   1732 C CB  . PRO   C 1 42 ? 18.631  -32.193 30.866  1.00 48.19  ? 41  PRO   C CB  1 
ATOM   1733 C CG  . PRO   C 1 42 ? 19.216  -30.967 31.515  1.00 48.66  ? 41  PRO   C CG  1 
ATOM   1734 C CD  . PRO   C 1 42 ? 20.707  -31.268 31.468  1.00 53.85  ? 41  PRO   C CD  1 
ATOM   1735 N N   . ILE   C 1 43 ? 18.821  -32.163 27.336  1.00 44.12  ? 42  ILE   C N   1 
ATOM   1736 C CA  . ILE   C 1 43 ? 18.486  -31.462 26.104  1.00 38.61  ? 42  ILE   C CA  1 
ATOM   1737 C C   . ILE   C 1 43 ? 17.046  -31.740 25.679  1.00 45.32  ? 42  ILE   C C   1 
ATOM   1738 O O   . ILE   C 1 43 ? 16.633  -32.891 25.537  1.00 51.14  ? 42  ILE   C O   1 
ATOM   1739 C CB  . ILE   C 1 43 ? 19.435  -31.872 24.970  1.00 37.09  ? 42  ILE   C CB  1 
ATOM   1740 C CG1 . ILE   C 1 43 ? 20.919  -31.574 25.294  1.00 43.82  ? 42  ILE   C CG1 1 
ATOM   1741 C CG2 . ILE   C 1 43 ? 18.961  -31.316 23.621  1.00 32.64  ? 42  ILE   C CG2 1 
ATOM   1742 C CD1 . ILE   C 1 43 ? 21.248  -30.142 25.706  1.00 38.03  ? 42  ILE   C CD1 1 
ATOM   1743 N N   . PHE   C 1 44 ? 16.306  -30.655 25.407  1.00 53.72  ? 43  PHE   C N   1 
ATOM   1744 C CA  . PHE   C 1 44 ? 15.063  -30.699 24.658  1.00 44.10  ? 43  PHE   C CA  1 
ATOM   1745 C C   . PHE   C 1 44 ? 15.322  -30.286 23.205  1.00 44.21  ? 43  PHE   C C   1 
ATOM   1746 O O   . PHE   C 1 44 ? 15.782  -29.181 22.940  1.00 49.06  ? 43  PHE   C O   1 
ATOM   1747 C CB  . PHE   C 1 44 ? 14.125  -29.719 25.365  1.00 52.13  ? 43  PHE   C CB  1 
ATOM   1748 C CG  . PHE   C 1 44 ? 12.750  -29.650 24.712  1.00 67.27  ? 43  PHE   C CG  1 
ATOM   1749 C CD1 . PHE   C 1 44 ? 11.840  -30.709 24.856  1.00 62.72  ? 43  PHE   C CD1 1 
ATOM   1750 C CD2 . PHE   C 1 44 ? 12.379  -28.540 23.949  1.00 56.03  ? 43  PHE   C CD2 1 
ATOM   1751 C CE1 . PHE   C 1 44 ? 10.588  -30.658 24.256  1.00 66.34  ? 43  PHE   C CE1 1 
ATOM   1752 C CE2 . PHE   C 1 44 ? 11.131  -28.501 23.339  1.00 61.03  ? 43  PHE   C CE2 1 
ATOM   1753 C CZ  . PHE   C 1 44 ? 10.238  -29.552 23.500  1.00 67.86  ? 43  PHE   C CZ  1 
ATOM   1754 N N   . PHE   C 1 45 ? 15.016  -31.178 22.262  1.00 42.51  ? 44  PHE   C N   1 
ATOM   1755 C CA  . PHE   C 1 45 ? 15.075  -30.883 20.836  1.00 48.20  ? 44  PHE   C CA  1 
ATOM   1756 C C   . PHE   C 1 45 ? 13.721  -30.328 20.389  1.00 51.47  ? 44  PHE   C C   1 
ATOM   1757 O O   . PHE   C 1 45 ? 12.693  -30.922 20.689  1.00 52.20  ? 44  PHE   C O   1 
ATOM   1758 C CB  . PHE   C 1 45 ? 15.393  -32.150 20.033  1.00 42.23  ? 44  PHE   C CB  1 
ATOM   1759 C CG  . PHE   C 1 45 ? 16.652  -32.889 20.478  1.00 46.75  ? 44  PHE   C CG  1 
ATOM   1760 C CD1 . PHE   C 1 45 ? 17.882  -32.618 19.887  1.00 46.22  ? 44  PHE   C CD1 1 
ATOM   1761 C CD2 . PHE   C 1 45 ? 16.620  -33.818 21.524  1.00 42.61  ? 44  PHE   C CD2 1 
ATOM   1762 C CE1 . PHE   C 1 45 ? 19.038  -33.270 20.324  1.00 46.82  ? 44  PHE   C CE1 1 
ATOM   1763 C CE2 . PHE   C 1 45 ? 17.775  -34.475 21.941  1.00 41.92  ? 44  PHE   C CE2 1 
ATOM   1764 C CZ  . PHE   C 1 45 ? 18.984  -34.197 21.347  1.00 40.31  ? 44  PHE   C CZ  1 
ATOM   1765 N N   . PHE   C 1 46 ? 13.729  -29.179 19.689  1.00 56.66  ? 45  PHE   C N   1 
ATOM   1766 C CA  . PHE   C 1 46 ? 12.546  -28.614 19.042  1.00 52.36  ? 45  PHE   C CA  1 
ATOM   1767 C C   . PHE   C 1 46 ? 12.135  -29.497 17.861  1.00 54.28  ? 45  PHE   C C   1 
ATOM   1768 O O   . PHE   C 1 46 ? 12.964  -30.229 17.307  1.00 52.04  ? 45  PHE   C O   1 
ATOM   1769 C CB  . PHE   C 1 46 ? 12.765  -27.149 18.636  1.00 43.04  ? 45  PHE   C CB  1 
ATOM   1770 C CG  . PHE   C 1 46 ? 13.160  -26.243 19.793  1.00 46.21  ? 45  PHE   C CG  1 
ATOM   1771 C CD1 . PHE   C 1 46 ? 12.234  -25.891 20.774  1.00 48.30  ? 45  PHE   C CD1 1 
ATOM   1772 C CD2 . PHE   C 1 46 ? 14.459  -25.749 19.912  1.00 45.92  ? 45  PHE   C CD2 1 
ATOM   1773 C CE1 . PHE   C 1 46 ? 12.603  -25.074 21.837  1.00 51.38  ? 45  PHE   C CE1 1 
ATOM   1774 C CE2 . PHE   C 1 46 ? 14.824  -24.935 20.975  1.00 45.22  ? 45  PHE   C CE2 1 
ATOM   1775 C CZ  . PHE   C 1 46 ? 13.895  -24.589 21.930  1.00 50.67  ? 45  PHE   C CZ  1 
ATOM   1776 N N   . GLY   C 1 47 ? 10.846  -29.433 17.484  1.00 53.51  ? 46  GLY   C N   1 
ATOM   1777 C CA  . GLY   C 1 47 ? 10.346  -30.219 16.362  1.00 48.79  ? 46  GLY   C CA  1 
ATOM   1778 C C   . GLY   C 1 47 ? 9.881   -31.613 16.791  1.00 55.96  ? 46  GLY   C C   1 
ATOM   1779 O O   . GLY   C 1 47 ? 8.675   -31.843 16.905  1.00 57.09  ? 46  GLY   C O   1 
ATOM   1780 N N   . THR   C 1 48 ? 10.831  -32.526 17.052  1.00 49.51  ? 47  THR   C N   1 
ATOM   1781 C CA  . THR   C 1 48 ? 10.502  -33.812 17.660  1.00 52.83  ? 47  THR   C CA  1 
ATOM   1782 C C   . THR   C 1 48 ? 9.929   -33.623 19.073  1.00 51.26  ? 47  THR   C C   1 
ATOM   1783 O O   . THR   C 1 48 ? 8.955   -34.285 19.457  1.00 48.16  ? 47  THR   C O   1 
ATOM   1784 C CB  . THR   C 1 48 ? 11.724  -34.733 17.691  1.00 46.42  ? 47  THR   C CB  1 
ATOM   1785 O OG1 . THR   C 1 48 ? 12.557  -34.176 18.705  1.00 42.92  ? 47  THR   C OG1 1 
ATOM   1786 C CG2 . THR   C 1 48 ? 12.390  -34.887 16.335  1.00 39.67  ? 47  THR   C CG2 1 
ATOM   1787 N N   . HIS   C 1 49 ? 10.550  -32.717 19.837  1.00 50.03  ? 48  HIS   C N   1 
ATOM   1788 C CA  . HIS   C 1 49 ? 10.258  -32.467 21.248  1.00 58.13  ? 48  HIS   C CA  1 
ATOM   1789 C C   . HIS   C 1 49 ? 10.705  -33.638 22.116  1.00 50.36  ? 48  HIS   C C   1 
ATOM   1790 O O   . HIS   C 1 49 ? 10.137  -33.865 23.178  1.00 55.13  ? 48  HIS   C O   1 
ATOM   1791 C CB  . HIS   C 1 49 ? 8.793   -32.087 21.535  1.00 66.63  ? 48  HIS   C CB  1 
ATOM   1792 C CG  . HIS   C 1 49 ? 8.177   -31.092 20.608  1.00 66.96  ? 48  HIS   C CG  1 
ATOM   1793 N ND1 . HIS   C 1 49 ? 7.190   -31.437 19.709  1.00 67.10  ? 48  HIS   C ND1 1 
ATOM   1794 C CD2 . HIS   C 1 49 ? 8.386   -29.781 20.445  1.00 70.33  ? 48  HIS   C CD2 1 
ATOM   1795 C CE1 . HIS   C 1 49 ? 6.832   -30.363 19.019  1.00 71.28  ? 48  HIS   C CE1 1 
ATOM   1796 N NE2 . HIS   C 1 49 ? 7.548   -29.347 19.449  1.00 71.71  ? 48  HIS   C NE2 1 
ATOM   1797 N N   . GLU   C 1 50 ? 11.743  -34.353 21.674  1.00 49.88  ? 49  GLU   C N   1 
ATOM   1798 C CA  . GLU   C 1 50 ? 12.251  -35.487 22.427  1.00 53.39  ? 49  GLU   C CA  1 
ATOM   1799 C C   . GLU   C 1 50 ? 13.309  -34.972 23.393  1.00 59.71  ? 49  GLU   C C   1 
ATOM   1800 O O   . GLU   C 1 50 ? 13.553  -33.764 23.438  1.00 51.86  ? 49  GLU   C O   1 
ATOM   1801 C CB  . GLU   C 1 50 ? 12.791  -36.566 21.493  1.00 57.47  ? 49  GLU   C CB  1 
ATOM   1802 C CG  . GLU   C 1 50 ? 11.758  -37.644 21.170  1.00 63.24  ? 49  GLU   C CG  1 
ATOM   1803 C CD  . GLU   C 1 50 ? 12.073  -38.524 19.973  1.00 65.81  ? 49  GLU   C CD  1 
ATOM   1804 O OE1 . GLU   C 1 50 ? 13.236  -38.952 19.791  1.00 68.47  ? 49  GLU   C OE1 1 
ATOM   1805 O OE2 . GLU   C 1 50 ? 11.128  -38.799 19.216  1.00 67.35  ? 49  GLU   C OE2 1 
ATOM   1806 N N   . THR   C 1 51 ? 13.889  -35.878 24.195  1.00 50.45  ? 50  THR   C N   1 
ATOM   1807 C CA  . THR   C 1 51 ? 14.918  -35.467 25.145  1.00 52.20  ? 50  THR   C CA  1 
ATOM   1808 C C   . THR   C 1 51 ? 16.061  -36.485 25.128  1.00 49.89  ? 50  THR   C C   1 
ATOM   1809 O O   . THR   C 1 51 ? 15.924  -37.546 24.529  1.00 56.05  ? 50  THR   C O   1 
ATOM   1810 C CB  . THR   C 1 51 ? 14.365  -35.192 26.550  1.00 43.17  ? 50  THR   C CB  1 
ATOM   1811 O OG1 . THR   C 1 51 ? 13.549  -36.326 26.830  1.00 38.43  ? 50  THR   C OG1 1 
ATOM   1812 C CG2 . THR   C 1 51 ? 13.572  -33.895 26.664  1.00 36.31  ? 50  THR   C CG2 1 
ATOM   1813 N N   . ALA   C 1 52 ? 17.197  -36.113 25.732  1.00 48.75  ? 51  ALA   C N   1 
ATOM   1814 C CA  . ALA   C 1 52 ? 18.418  -36.908 25.751  1.00 49.70  ? 51  ALA   C CA  1 
ATOM   1815 C C   . ALA   C 1 52 ? 19.427  -36.222 26.654  1.00 49.43  ? 51  ALA   C C   1 
ATOM   1816 O O   . ALA   C 1 52 ? 19.236  -35.058 27.011  1.00 51.56  ? 51  ALA   C O   1 
ATOM   1817 C CB  . ALA   C 1 52 ? 18.998  -37.073 24.353  1.00 48.92  ? 51  ALA   C CB  1 
ATOM   1818 N N   . PHE   C 1 53 ? 20.508  -36.947 26.966  1.00 53.91  ? 52  PHE   C N   1 
ATOM   1819 C CA  . PHE   C 1 53 ? 21.658  -36.382 27.653  1.00 56.98  ? 52  PHE   C CA  1 
ATOM   1820 C C   . PHE   C 1 53 ? 22.821  -36.221 26.683  1.00 55.78  ? 52  PHE   C C   1 
ATOM   1821 O O   . PHE   C 1 53 ? 23.199  -37.191 26.023  1.00 46.63  ? 52  PHE   C O   1 
ATOM   1822 C CB  . PHE   C 1 53 ? 22.016  -37.310 28.811  1.00 50.72  ? 52  PHE   C CB  1 
ATOM   1823 C CG  . PHE   C 1 53 ? 21.100  -37.080 30.000  1.00 55.31  ? 52  PHE   C CG  1 
ATOM   1824 C CD1 . PHE   C 1 53 ? 20.910  -35.797 30.509  1.00 61.26  ? 52  PHE   C CD1 1 
ATOM   1825 C CD2 . PHE   C 1 53 ? 20.421  -38.138 30.590  1.00 57.97  ? 52  PHE   C CD2 1 
ATOM   1826 C CE1 . PHE   C 1 53 ? 20.082  -35.584 31.599  1.00 60.62  ? 52  PHE   C CE1 1 
ATOM   1827 C CE2 . PHE   C 1 53 ? 19.606  -37.922 31.685  1.00 55.59  ? 52  PHE   C CE2 1 
ATOM   1828 C CZ  . PHE   C 1 53 ? 19.432  -36.647 32.180  1.00 59.47  ? 52  PHE   C CZ  1 
ATOM   1829 N N   . LEU   C 1 54 ? 23.366  -34.993 26.615  1.00 51.00  ? 53  LEU   C N   1 
ATOM   1830 C CA  . LEU   C 1 54 ? 24.522  -34.733 25.768  1.00 56.94  ? 53  LEU   C CA  1 
ATOM   1831 C C   . LEU   C 1 54 ? 25.621  -34.040 26.572  1.00 55.71  ? 53  LEU   C C   1 
ATOM   1832 O O   . LEU   C 1 54 ? 25.325  -33.270 27.487  1.00 47.61  ? 53  LEU   C O   1 
ATOM   1833 C CB  . LEU   C 1 54 ? 24.216  -33.981 24.468  1.00 54.00  ? 53  LEU   C CB  1 
ATOM   1834 C CG  . LEU   C 1 54 ? 23.250  -34.640 23.478  1.00 53.54  ? 53  LEU   C CG  1 
ATOM   1835 C CD1 . LEU   C 1 54 ? 22.947  -33.685 22.344  1.00 49.70  ? 53  LEU   C CD1 1 
ATOM   1836 C CD2 . LEU   C 1 54 ? 23.755  -35.965 22.924  1.00 54.75  ? 53  LEU   C CD2 1 
ATOM   1837 N N   . GLY   C 1 55 ? 26.880  -34.349 26.200  1.00 56.57  ? 54  GLY   C N   1 
ATOM   1838 C CA  . GLY   C 1 55 ? 28.086  -33.679 26.663  1.00 47.77  ? 54  GLY   C CA  1 
ATOM   1839 C C   . GLY   C 1 55 ? 28.274  -32.349 25.937  1.00 57.77  ? 54  GLY   C C   1 
ATOM   1840 O O   . GLY   C 1 55 ? 27.642  -32.110 24.903  1.00 61.95  ? 54  GLY   C O   1 
ATOM   1841 N N   . PRO   C 1 56 ? 29.122  -31.429 26.456  1.00 54.05  ? 55  PRO   C N   1 
ATOM   1842 C CA  . PRO   C 1 56 ? 29.227  -30.091 25.875  1.00 60.74  ? 55  PRO   C CA  1 
ATOM   1843 C C   . PRO   C 1 56 ? 29.898  -30.116 24.506  1.00 53.23  ? 55  PRO   C C   1 
ATOM   1844 O O   . PRO   C 1 56 ? 29.719  -29.207 23.700  1.00 55.77  ? 55  PRO   C O   1 
ATOM   1845 C CB  . PRO   C 1 56 ? 30.021  -29.318 26.929  1.00 57.41  ? 55  PRO   C CB  1 
ATOM   1846 C CG  . PRO   C 1 56 ? 30.866  -30.392 27.574  1.00 55.37  ? 55  PRO   C CG  1 
ATOM   1847 C CD  . PRO   C 1 56 ? 29.958  -31.600 27.654  1.00 52.84  ? 55  PRO   C CD  1 
ATOM   1848 N N   . LYS   C 1 57 ? 30.647  -31.186 24.253  1.00 49.71  ? 56  LYS   C N   1 
ATOM   1849 C CA  . LYS   C 1 57 ? 31.254  -31.410 22.950  1.00 56.27  ? 56  LYS   C CA  1 
ATOM   1850 C C   . LYS   C 1 57 ? 30.193  -31.257 21.861  1.00 50.79  ? 56  LYS   C C   1 
ATOM   1851 O O   . LYS   C 1 57 ? 30.522  -30.955 20.719  1.00 40.64  ? 56  LYS   C O   1 
ATOM   1852 C CB  . LYS   C 1 57 ? 31.832  -32.836 22.898  1.00 57.54  ? 56  LYS   C CB  1 
ATOM   1853 N N   . ASP   C 1 58 ? 28.928  -31.481 22.246  1.00 56.70  ? 57  ASP   C N   1 
ATOM   1854 C CA  . ASP   C 1 58 ? 27.834  -31.781 21.332  1.00 55.95  ? 57  ASP   C CA  1 
ATOM   1855 C C   . ASP   C 1 58 ? 26.903  -30.582 21.197  1.00 54.49  ? 57  ASP   C C   1 
ATOM   1856 O O   . ASP   C 1 58 ? 25.906  -30.655 20.485  1.00 59.36  ? 57  ASP   C O   1 
ATOM   1857 C CB  . ASP   C 1 58 ? 27.106  -33.044 21.769  1.00 53.74  ? 57  ASP   C CB  1 
ATOM   1858 C CG  . ASP   C 1 58 ? 27.970  -34.298 21.756  1.00 56.42  ? 57  ASP   C CG  1 
ATOM   1859 O OD1 . ASP   C 1 58 ? 29.041  -34.250 21.113  1.00 56.48  ? 57  ASP   C OD1 1 
ATOM   1860 O OD2 . ASP   C 1 58 ? 27.583  -35.304 22.401  1.00 46.95  ? 57  ASP   C OD2 1 
ATOM   1861 N N   . LEU   C 1 59 ? 27.264  -29.476 21.860  1.00 54.26  ? 58  LEU   C N   1 
ATOM   1862 C CA  . LEU   C 1 59 ? 26.366  -28.356 22.077  1.00 51.62  ? 58  LEU   C CA  1 
ATOM   1863 C C   . LEU   C 1 59 ? 26.959  -27.105 21.442  1.00 54.18  ? 58  LEU   C C   1 
ATOM   1864 O O   . LEU   C 1 59 ? 28.167  -26.909 21.477  1.00 63.56  ? 58  LEU   C O   1 
ATOM   1865 C CB  . LEU   C 1 59 ? 26.163  -28.210 23.584  1.00 45.54  ? 58  LEU   C CB  1 
ATOM   1866 C CG  . LEU   C 1 59 ? 25.426  -29.370 24.264  1.00 47.63  ? 58  LEU   C CG  1 
ATOM   1867 C CD1 . LEU   C 1 59 ? 25.329  -29.165 25.771  1.00 48.97  ? 58  LEU   C CD1 1 
ATOM   1868 C CD2 . LEU   C 1 59 ? 24.036  -29.550 23.710  1.00 41.34  ? 58  LEU   C CD2 1 
ATOM   1869 N N   . PHE   C 1 60 ? 26.102  -26.278 20.833  1.00 53.71  ? 59  PHE   C N   1 
ATOM   1870 C CA  . PHE   C 1 60 ? 26.571  -25.126 20.080  1.00 54.31  ? 59  PHE   C CA  1 
ATOM   1871 C C   . PHE   C 1 60 ? 25.620  -23.949 20.259  1.00 57.08  ? 59  PHE   C C   1 
ATOM   1872 O O   . PHE   C 1 60 ? 24.452  -24.024 19.870  1.00 60.72  ? 59  PHE   C O   1 
ATOM   1873 C CB  . PHE   C 1 60 ? 26.655  -25.452 18.588  1.00 51.10  ? 59  PHE   C CB  1 
ATOM   1874 C CG  . PHE   C 1 60 ? 27.701  -26.497 18.250  1.00 46.22  ? 59  PHE   C CG  1 
ATOM   1875 C CD1 . PHE   C 1 60 ? 27.372  -27.847 18.231  1.00 46.05  ? 59  PHE   C CD1 1 
ATOM   1876 C CD2 . PHE   C 1 60 ? 29.012  -26.115 17.963  1.00 53.00  ? 59  PHE   C CD2 1 
ATOM   1877 C CE1 . PHE   C 1 60 ? 28.334  -28.797 17.919  1.00 48.45  ? 59  PHE   C CE1 1 
ATOM   1878 C CE2 . PHE   C 1 60 ? 29.977  -27.059 17.652  1.00 49.91  ? 59  PHE   C CE2 1 
ATOM   1879 C CZ  . PHE   C 1 60 ? 29.627  -28.398 17.628  1.00 56.99  ? 59  PHE   C CZ  1 
ATOM   1880 N N   . PRO   C 1 61 ? 26.074  -22.835 20.874  1.00 52.60  ? 60  PRO   C N   1 
ATOM   1881 C CA  . PRO   C 1 61 ? 25.227  -21.647 21.004  1.00 50.38  ? 60  PRO   C CA  1 
ATOM   1882 C C   . PRO   C 1 61 ? 24.440  -21.357 19.724  1.00 50.90  ? 60  PRO   C C   1 
ATOM   1883 O O   . PRO   C 1 61 ? 24.969  -21.456 18.606  1.00 49.87  ? 60  PRO   C O   1 
ATOM   1884 C CB  . PRO   C 1 61 ? 26.212  -20.529 21.404  1.00 54.83  ? 60  PRO   C CB  1 
ATOM   1885 C CG  . PRO   C 1 61 ? 27.330  -21.277 22.111  1.00 59.63  ? 60  PRO   C CG  1 
ATOM   1886 C CD  . PRO   C 1 61 ? 27.377  -22.695 21.542  1.00 51.42  ? 60  PRO   C CD  1 
ATOM   1887 N N   . TYR   C 1 62 ? 23.156  -21.026 19.928  1.00 51.93  ? 61  TYR   C N   1 
ATOM   1888 C CA  . TYR   C 1 62 ? 22.179  -20.843 18.870  1.00 53.93  ? 61  TYR   C CA  1 
ATOM   1889 C C   . TYR   C 1 62 ? 22.638  -19.708 17.961  1.00 53.79  ? 61  TYR   C C   1 
ATOM   1890 O O   . TYR   C 1 62 ? 22.964  -19.972 16.806  1.00 47.03  ? 61  TYR   C O   1 
ATOM   1891 C CB  . TYR   C 1 62 ? 20.751  -20.650 19.393  1.00 55.96  ? 61  TYR   C CB  1 
ATOM   1892 C CG  . TYR   C 1 62 ? 19.763  -20.328 18.283  1.00 52.75  ? 61  TYR   C CG  1 
ATOM   1893 C CD1 . TYR   C 1 62 ? 19.709  -21.118 17.136  1.00 54.07  ? 61  TYR   C CD1 1 
ATOM   1894 C CD2 . TYR   C 1 62 ? 18.926  -19.217 18.358  1.00 54.93  ? 61  TYR   C CD2 1 
ATOM   1895 C CE1 . TYR   C 1 62 ? 18.839  -20.820 16.099  1.00 55.60  ? 61  TYR   C CE1 1 
ATOM   1896 C CE2 . TYR   C 1 62 ? 18.038  -18.916 17.333  1.00 55.48  ? 61  TYR   C CE2 1 
ATOM   1897 C CZ  . TYR   C 1 62 ? 18.001  -19.718 16.201  1.00 53.51  ? 61  TYR   C CZ  1 
ATOM   1898 O OH  . TYR   C 1 62 ? 17.165  -19.447 15.164  1.00 49.10  ? 61  TYR   C OH  1 
ATOM   1899 N N   . ASP   C 1 63 ? 22.711  -18.488 18.522  1.00 57.24  ? 62  ASP   C N   1 
ATOM   1900 C CA  . ASP   C 1 63 ? 23.187  -17.285 17.845  1.00 65.70  ? 62  ASP   C CA  1 
ATOM   1901 C C   . ASP   C 1 63 ? 24.577  -17.449 17.241  1.00 61.67  ? 62  ASP   C C   1 
ATOM   1902 O O   . ASP   C 1 63 ? 24.796  -16.986 16.121  1.00 66.90  ? 62  ASP   C O   1 
ATOM   1903 C CB  . ASP   C 1 63 ? 23.176  -16.051 18.732  1.00 73.05  ? 62  ASP   C CB  1 
ATOM   1904 C CG  . ASP   C 1 63 ? 21.944  -15.176 18.566  1.00 76.43  ? 62  ASP   C CG  1 
ATOM   1905 O OD1 . ASP   C 1 63 ? 21.135  -15.129 19.511  1.00 77.16  ? 62  ASP   C OD1 1 
ATOM   1906 O OD2 . ASP   C 1 63 ? 21.808  -14.552 17.488  1.00 69.81  ? 62  ASP   C OD2 1 
ATOM   1907 N N   . LYS   C 1 64 ? 25.507  -18.089 17.967  1.00 52.67  ? 63  LYS   C N   1 
ATOM   1908 C CA  . LYS   C 1 64 ? 26.857  -18.270 17.439  1.00 51.07  ? 63  LYS   C CA  1 
ATOM   1909 C C   . LYS   C 1 64 ? 26.873  -19.131 16.164  1.00 49.62  ? 63  LYS   C C   1 
ATOM   1910 O O   . LYS   C 1 64 ? 27.638  -18.844 15.249  1.00 50.09  ? 63  LYS   C O   1 
ATOM   1911 C CB  . LYS   C 1 64 ? 27.905  -18.619 18.513  1.00 48.67  ? 63  LYS   C CB  1 
ATOM   1912 N N   . SER   C 1 65 ? 26.020  -20.169 16.084  1.00 55.39  ? 64  SER   C N   1 
ATOM   1913 C CA  . SER   C 1 65 ? 26.203  -21.279 15.146  1.00 53.52  ? 64  SER   C CA  1 
ATOM   1914 C C   . SER   C 1 65 ? 25.077  -21.391 14.118  1.00 50.01  ? 64  SER   C C   1 
ATOM   1915 O O   . SER   C 1 65 ? 25.179  -22.166 13.172  1.00 37.16  ? 64  SER   C O   1 
ATOM   1916 C CB  . SER   C 1 65 ? 26.317  -22.571 15.898  1.00 52.14  ? 64  SER   C CB  1 
ATOM   1917 O OG  . SER   C 1 65 ? 25.102  -22.768 16.597  1.00 47.36  ? 64  SER   C OG  1 
ATOM   1918 N N   . LYS   C 1 66 ? 23.994  -20.629 14.333  1.00 57.98  ? 65  LYS   C N   1 
ATOM   1919 C CA  . LYS   C 1 66 ? 22.805  -20.688 13.501  1.00 61.83  ? 65  LYS   C CA  1 
ATOM   1920 C C   . LYS   C 1 66 ? 23.182  -20.630 12.023  1.00 64.08  ? 65  LYS   C C   1 
ATOM   1921 O O   . LYS   C 1 66 ? 22.832  -21.531 11.265  1.00 64.87  ? 65  LYS   C O   1 
ATOM   1922 C CB  . LYS   C 1 66 ? 21.714  -19.686 13.908  1.00 62.71  ? 65  LYS   C CB  1 
ATOM   1923 C CG  . LYS   C 1 66 ? 22.049  -18.204 14.002  1.00 67.65  ? 65  LYS   C CG  1 
ATOM   1924 C CD  . LYS   C 1 66 ? 20.879  -17.439 14.612  1.00 76.07  ? 65  LYS   C CD  1 
ATOM   1925 C CE  . LYS   C 1 66 ? 21.013  -15.953 14.548  1.00 76.70  ? 65  LYS   C CE  1 
ATOM   1926 N NZ  . LYS   C 1 66 ? 19.805  -15.296 15.052  1.00 81.43  ? 65  LYS   C NZ  1 
ATOM   1927 N N   . ASP   C 1 67 ? 23.913  -19.582 11.623  1.00 65.09  ? 66  ASP   C N   1 
ATOM   1928 C CA  . ASP   C 1 67 ? 24.246  -19.406 10.217  1.00 60.86  ? 66  ASP   C CA  1 
ATOM   1929 C C   . ASP   C 1 67 ? 24.789  -20.713 9.645   1.00 55.70  ? 66  ASP   C C   1 
ATOM   1930 O O   . ASP   C 1 67 ? 24.606  -20.995 8.463   1.00 59.22  ? 66  ASP   C O   1 
ATOM   1931 C CB  . ASP   C 1 67 ? 25.094  -18.176 9.932   1.00 57.50  ? 66  ASP   C CB  1 
ATOM   1932 C CG  . ASP   C 1 67 ? 26.393  -18.007 10.706  1.00 63.73  ? 66  ASP   C CG  1 
ATOM   1933 O OD1 . ASP   C 1 67 ? 27.160  -18.994 10.860  1.00 59.37  ? 66  ASP   C OD1 1 
ATOM   1934 O OD2 . ASP   C 1 67 ? 26.655  -16.856 11.107  1.00 74.77  ? 66  ASP   C OD2 1 
ATOM   1935 N N   . LYS   C 1 68 ? 25.417  -21.525 10.499  1.00 42.78  ? 67  LYS   C N   1 
ATOM   1936 C CA  . LYS   C 1 68 ? 25.991  -22.760 10.001  1.00 49.87  ? 67  LYS   C CA  1 
ATOM   1937 C C   . LYS   C 1 68 ? 24.920  -23.858 9.981   1.00 49.75  ? 67  LYS   C C   1 
ATOM   1938 O O   . LYS   C 1 68 ? 24.766  -24.559 8.973   1.00 45.03  ? 67  LYS   C O   1 
ATOM   1939 C CB  . LYS   C 1 68 ? 27.323  -23.066 10.715  1.00 55.16  ? 67  LYS   C CB  1 
ATOM   1940 C CG  . LYS   C 1 68 ? 28.014  -24.404 10.392  1.00 59.56  ? 67  LYS   C CG  1 
ATOM   1941 C CD  . LYS   C 1 68 ? 29.373  -24.658 11.052  1.00 68.89  ? 67  LYS   C CD  1 
ATOM   1942 C CE  . LYS   C 1 68 ? 29.885  -26.089 11.061  1.00 74.77  ? 67  LYS   C CE  1 
ATOM   1943 N NZ  . LYS   C 1 68 ? 29.959  -26.810 9.780   1.00 69.33  ? 67  LYS   C NZ  1 
ATOM   1944 N N   . TYR   C 1 69 ? 24.187  -23.999 11.099  1.00 44.98  ? 68  TYR   C N   1 
ATOM   1945 C CA  . TYR   C 1 69 ? 23.304  -25.138 11.296  1.00 47.78  ? 68  TYR   C CA  1 
ATOM   1946 C C   . TYR   C 1 69 ? 21.835  -24.756 11.122  1.00 50.40  ? 68  TYR   C C   1 
ATOM   1947 O O   . TYR   C 1 69 ? 20.984  -25.626 10.993  1.00 53.70  ? 68  TYR   C O   1 
ATOM   1948 C CB  . TYR   C 1 69 ? 23.540  -25.668 12.708  1.00 48.81  ? 68  TYR   C CB  1 
ATOM   1949 C CG  . TYR   C 1 69 ? 24.948  -26.177 12.965  1.00 51.86  ? 68  TYR   C CG  1 
ATOM   1950 C CD1 . TYR   C 1 69 ? 25.630  -26.936 12.022  1.00 50.80  ? 68  TYR   C CD1 1 
ATOM   1951 C CD2 . TYR   C 1 69 ? 25.582  -25.910 14.169  1.00 57.93  ? 68  TYR   C CD2 1 
ATOM   1952 C CE1 . TYR   C 1 69 ? 26.900  -27.428 12.277  1.00 54.18  ? 68  TYR   C CE1 1 
ATOM   1953 C CE2 . TYR   C 1 69 ? 26.858  -26.381 14.430  1.00 65.16  ? 68  TYR   C CE2 1 
ATOM   1954 C CZ  . TYR   C 1 69 ? 27.521  -27.139 13.481  1.00 61.49  ? 68  TYR   C CZ  1 
ATOM   1955 O OH  . TYR   C 1 69 ? 28.781  -27.585 13.761  1.00 64.15  ? 68  TYR   C OH  1 
ATOM   1956 N N   . GLY   C 1 70 ? 21.527  -23.459 11.162  1.00 50.53  ? 69  GLY   C N   1 
ATOM   1957 C CA  . GLY   C 1 70 ? 20.155  -23.021 10.976  1.00 57.64  ? 69  GLY   C CA  1 
ATOM   1958 C C   . GLY   C 1 70 ? 19.802  -23.053 9.493   1.00 59.88  ? 69  GLY   C C   1 
ATOM   1959 O O   . GLY   C 1 70 ? 19.458  -22.031 8.917   1.00 57.46  ? 69  GLY   C O   1 
ATOM   1960 N N   . LYS   C 1 71 ? 19.950  -24.228 8.876   1.00 59.61  ? 70  LYS   C N   1 
ATOM   1961 C CA  . LYS   C 1 71 ? 19.513  -24.425 7.505   1.00 64.54  ? 70  LYS   C CA  1 
ATOM   1962 C C   . LYS   C 1 71 ? 18.487  -25.555 7.514   1.00 66.03  ? 70  LYS   C C   1 
ATOM   1963 O O   . LYS   C 1 71 ? 18.591  -26.474 8.322   1.00 71.85  ? 70  LYS   C O   1 
ATOM   1964 C CB  . LYS   C 1 71 ? 20.702  -24.667 6.565   1.00 59.43  ? 70  LYS   C CB  1 
ATOM   1965 C CG  . LYS   C 1 71 ? 21.788  -25.545 7.167   1.00 65.07  ? 70  LYS   C CG  1 
ATOM   1966 C CD  . LYS   C 1 71 ? 22.747  -26.288 6.238   1.00 77.24  ? 70  LYS   C CD  1 
ATOM   1967 C CE  . LYS   C 1 71 ? 23.695  -27.184 7.008   1.00 77.76  ? 70  LYS   C CE  1 
ATOM   1968 N NZ  . LYS   C 1 71 ? 24.601  -27.990 6.178   1.00 76.87  ? 70  LYS   C NZ  1 
ATOM   1969 N N   . PRO   C 1 72 ? 17.413  -25.481 6.695   1.00 62.09  ? 71  PRO   C N   1 
ATOM   1970 C CA  . PRO   C 1 72 ? 16.428  -26.568 6.656   1.00 53.74  ? 71  PRO   C CA  1 
ATOM   1971 C C   . PRO   C 1 72 ? 17.009  -27.908 6.205   1.00 58.05  ? 71  PRO   C C   1 
ATOM   1972 O O   . PRO   C 1 72 ? 18.017  -27.953 5.501   1.00 55.87  ? 71  PRO   C O   1 
ATOM   1973 C CB  . PRO   C 1 72 ? 15.309  -26.075 5.734   1.00 51.00  ? 71  PRO   C CB  1 
ATOM   1974 C CG  . PRO   C 1 72 ? 15.594  -24.598 5.536   1.00 55.65  ? 71  PRO   C CG  1 
ATOM   1975 C CD  . PRO   C 1 72 ? 17.047  -24.311 5.876   1.00 52.28  ? 71  PRO   C CD  1 
ATOM   1976 N N   . ASN   C 1 73 ? 16.385  -28.998 6.663   1.00 54.63  ? 72  ASN   C N   1 
ATOM   1977 C CA  . ASN   C 1 73 ? 16.541  -30.301 6.032   1.00 56.71  ? 72  ASN   C CA  1 
ATOM   1978 C C   . ASN   C 1 73 ? 15.239  -31.072 6.219   1.00 48.78  ? 72  ASN   C C   1 
ATOM   1979 O O   . ASN   C 1 73 ? 14.304  -30.530 6.787   1.00 55.47  ? 72  ASN   C O   1 
ATOM   1980 C CB  . ASN   C 1 73 ? 17.862  -30.981 6.387   1.00 58.59  ? 72  ASN   C CB  1 
ATOM   1981 C CG  . ASN   C 1 73 ? 17.847  -31.695 7.714   1.00 60.21  ? 72  ASN   C CG  1 
ATOM   1982 O OD1 . ASN   C 1 73 ? 16.799  -31.838 8.354   1.00 67.70  ? 72  ASN   C OD1 1 
ATOM   1983 N ND2 . ASN   C 1 73 ? 19.006  -32.181 8.122   1.00 62.49  ? 72  ASN   C ND2 1 
ATOM   1984 N N   . LYS   C 1 74 ? 15.183  -32.324 5.750   1.00 53.74  ? 73  LYS   C N   1 
ATOM   1985 C CA  . LYS   C 1 74 ? 13.919  -33.048 5.675   1.00 53.47  ? 73  LYS   C CA  1 
ATOM   1986 C C   . LYS   C 1 74 ? 13.809  -34.117 6.756   1.00 55.65  ? 73  LYS   C C   1 
ATOM   1987 O O   . LYS   C 1 74 ? 12.906  -34.945 6.709   1.00 66.67  ? 73  LYS   C O   1 
ATOM   1988 C CB  . LYS   C 1 74 ? 13.699  -33.688 4.299   1.00 45.71  ? 73  LYS   C CB  1 
ATOM   1989 N N   . ARG   C 1 75 ? 14.742  -34.125 7.712   1.00 61.80  ? 74  ARG   C N   1 
ATOM   1990 C CA  . ARG   C 1 75 ? 14.661  -35.095 8.793   1.00 54.32  ? 74  ARG   C CA  1 
ATOM   1991 C C   . ARG   C 1 75 ? 13.415  -34.763 9.602   1.00 53.93  ? 74  ARG   C C   1 
ATOM   1992 O O   . ARG   C 1 75 ? 13.149  -33.588 9.843   1.00 52.09  ? 74  ARG   C O   1 
ATOM   1993 C CB  . ARG   C 1 75 ? 15.929  -35.160 9.652   1.00 54.21  ? 74  ARG   C CB  1 
ATOM   1994 C CG  . ARG   C 1 75 ? 17.188  -35.345 8.815   1.00 57.89  ? 74  ARG   C CG  1 
ATOM   1995 C CD  . ARG   C 1 75 ? 17.275  -36.692 8.096   1.00 59.43  ? 74  ARG   C CD  1 
ATOM   1996 N NE  . ARG   C 1 75 ? 17.635  -37.777 9.022   1.00 54.91  ? 74  ARG   C NE  1 
ATOM   1997 C CZ  . ARG   C 1 75 ? 18.845  -37.994 9.535   1.00 46.80  ? 74  ARG   C CZ  1 
ATOM   1998 N NH1 . ARG   C 1 75 ? 18.940  -38.708 10.634  1.00 49.74  ? 74  ARG   C NH1 1 
ATOM   1999 N NH2 . ARG   C 1 75 ? 19.927  -37.406 9.040   1.00 44.59  ? 74  ARG   C NH2 1 
ATOM   2000 N N   . LYS   C 1 76 ? 12.659  -35.806 9.969   1.00 48.09  ? 75  LYS   C N   1 
ATOM   2001 C CA  . LYS   C 1 76 ? 11.366  -35.665 10.611  1.00 51.00  ? 75  LYS   C CA  1 
ATOM   2002 C C   . LYS   C 1 76 ? 11.489  -34.745 11.824  1.00 51.85  ? 75  LYS   C C   1 
ATOM   2003 O O   . LYS   C 1 76 ? 12.254  -35.030 12.753  1.00 45.27  ? 75  LYS   C O   1 
ATOM   2004 C CB  . LYS   C 1 76 ? 10.765  -37.046 10.908  1.00 61.58  ? 75  LYS   C CB  1 
ATOM   2005 C CG  . LYS   C 1 76 ? 9.243   -37.156 10.812  1.00 71.44  ? 75  LYS   C CG  1 
ATOM   2006 C CD  . LYS   C 1 76 ? 8.576   -38.085 11.829  1.00 73.60  ? 75  LYS   C CD  1 
ATOM   2007 N N   . GLY   C 1 77 ? 10.749  -33.624 11.762  1.00 48.72  ? 76  GLY   C N   1 
ATOM   2008 C CA  . GLY   C 1 77 ? 10.570  -32.727 12.890  1.00 46.89  ? 76  GLY   C CA  1 
ATOM   2009 C C   . GLY   C 1 77 ? 11.486  -31.513 12.791  1.00 50.57  ? 76  GLY   C C   1 
ATOM   2010 O O   . GLY   C 1 77 ? 11.335  -30.557 13.553  1.00 54.30  ? 76  GLY   C O   1 
ATOM   2011 N N   . PHE   C 1 78 ? 12.410  -31.546 11.824  1.00 51.94  ? 77  PHE   C N   1 
ATOM   2012 C CA  . PHE   C 1 78 ? 13.542  -30.630 11.809  1.00 51.16  ? 77  PHE   C CA  1 
ATOM   2013 C C   . PHE   C 1 78 ? 13.042  -29.215 11.568  1.00 50.36  ? 77  PHE   C C   1 
ATOM   2014 O O   . PHE   C 1 78 ? 13.177  -28.354 12.428  1.00 56.53  ? 77  PHE   C O   1 
ATOM   2015 C CB  . PHE   C 1 78 ? 14.630  -30.974 10.787  1.00 46.56  ? 77  PHE   C CB  1 
ATOM   2016 C CG  . PHE   C 1 78 ? 15.905  -30.183 11.040  1.00 44.99  ? 77  PHE   C CG  1 
ATOM   2017 C CD1 . PHE   C 1 78 ? 16.082  -28.914 10.495  1.00 39.81  ? 77  PHE   C CD1 1 
ATOM   2018 C CD2 . PHE   C 1 78 ? 16.920  -30.703 11.837  1.00 42.13  ? 77  PHE   C CD2 1 
ATOM   2019 C CE1 . PHE   C 1 78 ? 17.236  -28.186 10.735  1.00 39.87  ? 77  PHE   C CE1 1 
ATOM   2020 C CE2 . PHE   C 1 78 ? 18.081  -29.972 12.068  1.00 42.63  ? 77  PHE   C CE2 1 
ATOM   2021 C CZ  . PHE   C 1 78 ? 18.235  -28.711 11.527  1.00 40.18  ? 77  PHE   C CZ  1 
ATOM   2022 N N   . ASN   C 1 79 ? 12.430  -29.009 10.404  1.00 47.97  ? 78  ASN   C N   1 
ATOM   2023 C CA  . ASN   C 1 79 ? 12.005  -27.690 9.990   1.00 43.81  ? 78  ASN   C CA  1 
ATOM   2024 C C   . ASN   C 1 79 ? 11.052  -27.120 11.026  1.00 43.38  ? 78  ASN   C C   1 
ATOM   2025 O O   . ASN   C 1 79 ? 11.158  -25.949 11.381  1.00 46.30  ? 78  ASN   C O   1 
ATOM   2026 C CB  . ASN   C 1 79 ? 11.448  -27.722 8.576   1.00 44.68  ? 78  ASN   C CB  1 
ATOM   2027 C CG  . ASN   C 1 79 ? 12.540  -28.070 7.590   1.00 45.39  ? 78  ASN   C CG  1 
ATOM   2028 O OD1 . ASN   C 1 79 ? 13.719  -28.027 7.955   1.00 46.77  ? 78  ASN   C OD1 1 
ATOM   2029 N ND2 . ASN   C 1 79 ? 12.196  -28.360 6.343   1.00 47.16  ? 78  ASN   C ND2 1 
ATOM   2030 N N   . GLU   C 1 80 ? 10.140  -27.957 11.518  1.00 48.02  ? 79  GLU   C N   1 
ATOM   2031 C CA  . GLU   C 1 80 ? 9.232   -27.531 12.571  1.00 51.44  ? 79  GLU   C CA  1 
ATOM   2032 C C   . GLU   C 1 80 ? 10.040  -27.079 13.775  1.00 46.16  ? 79  GLU   C C   1 
ATOM   2033 O O   . GLU   C 1 80 ? 9.678   -26.092 14.410  1.00 45.96  ? 79  GLU   C O   1 
ATOM   2034 C CB  . GLU   C 1 80 ? 8.314   -28.646 13.062  1.00 54.38  ? 79  GLU   C CB  1 
ATOM   2035 C CG  . GLU   C 1 80 ? 7.216   -28.130 13.990  1.00 61.96  ? 79  GLU   C CG  1 
ATOM   2036 C CD  . GLU   C 1 80 ? 6.041   -29.079 14.218  1.00 72.87  ? 79  GLU   C CD  1 
ATOM   2037 O OE1 . GLU   C 1 80 ? 6.159   -30.278 13.869  1.00 72.93  ? 79  GLU   C OE1 1 
ATOM   2038 O OE2 . GLU   C 1 80 ? 4.991   -28.627 14.734  1.00 71.14  ? 79  GLU   C OE2 1 
ATOM   2039 N N   . GLY   C 1 81 ? 11.139  -27.804 14.032  1.00 43.03  ? 80  GLY   C N   1 
ATOM   2040 C CA  . GLY   C 1 81 ? 12.057  -27.545 15.134  1.00 43.01  ? 80  GLY   C CA  1 
ATOM   2041 C C   . GLY   C 1 81 ? 12.814  -26.236 14.938  1.00 44.83  ? 80  GLY   C C   1 
ATOM   2042 O O   . GLY   C 1 81 ? 13.126  -25.555 15.918  1.00 43.72  ? 80  GLY   C O   1 
ATOM   2043 N N   . LEU   C 1 82 ? 13.088  -25.892 13.666  1.00 40.99  ? 81  LEU   C N   1 
ATOM   2044 C CA  . LEU   C 1 82 ? 13.652  -24.599 13.301  1.00 41.87  ? 81  LEU   C CA  1 
ATOM   2045 C C   . LEU   C 1 82 ? 12.682  -23.458 13.624  1.00 45.11  ? 81  LEU   C C   1 
ATOM   2046 O O   . LEU   C 1 82 ? 13.092  -22.407 14.131  1.00 46.67  ? 81  LEU   C O   1 
ATOM   2047 C CB  . LEU   C 1 82 ? 14.064  -24.575 11.829  1.00 42.01  ? 81  LEU   C CB  1 
ATOM   2048 C CG  . LEU   C 1 82 ? 15.427  -25.189 11.495  1.00 44.50  ? 81  LEU   C CG  1 
ATOM   2049 C CD1 . LEU   C 1 82 ? 15.730  -25.084 9.987   1.00 43.16  ? 81  LEU   C CD1 1 
ATOM   2050 C CD2 . LEU   C 1 82 ? 16.493  -24.489 12.312  1.00 41.85  ? 81  LEU   C CD2 1 
ATOM   2051 N N   . TRP   C 1 83 ? 11.398  -23.653 13.294  1.00 39.95  ? 82  TRP   C N   1 
ATOM   2052 C CA  . TRP   C 1 83 ? 10.416  -22.624 13.584  1.00 45.94  ? 82  TRP   C CA  1 
ATOM   2053 C C   . TRP   C 1 83 ? 10.350  -22.367 15.091  1.00 45.52  ? 82  TRP   C C   1 
ATOM   2054 O O   . TRP   C 1 83 ? 10.243  -21.230 15.526  1.00 42.50  ? 82  TRP   C O   1 
ATOM   2055 C CB  . TRP   C 1 83 ? 9.039   -23.008 13.034  1.00 44.89  ? 82  TRP   C CB  1 
ATOM   2056 C CG  . TRP   C 1 83 ? 7.999   -21.914 13.130  1.00 53.24  ? 82  TRP   C CG  1 
ATOM   2057 C CD1 . TRP   C 1 83 ? 7.588   -21.093 12.120  1.00 50.93  ? 82  TRP   C CD1 1 
ATOM   2058 C CD2 . TRP   C 1 83 ? 7.222   -21.531 14.290  1.00 50.53  ? 82  TRP   C CD2 1 
ATOM   2059 N NE1 . TRP   C 1 83 ? 6.608   -20.246 12.563  1.00 55.03  ? 82  TRP   C NE1 1 
ATOM   2060 C CE2 . TRP   C 1 83 ? 6.364   -20.489 13.885  1.00 50.22  ? 82  TRP   C CE2 1 
ATOM   2061 C CE3 . TRP   C 1 83 ? 7.153   -21.976 15.617  1.00 56.23  ? 82  TRP   C CE3 1 
ATOM   2062 C CZ2 . TRP   C 1 83 ? 5.461   -19.889 14.761  1.00 59.39  ? 82  TRP   C CZ2 1 
ATOM   2063 C CZ3 . TRP   C 1 83 ? 6.267   -21.381 16.487  1.00 51.83  ? 82  TRP   C CZ3 1 
ATOM   2064 C CH2 . TRP   C 1 83 ? 5.426   -20.354 16.058  1.00 58.19  ? 82  TRP   C CH2 1 
ATOM   2065 N N   . GLU   C 1 84 ? 10.412  -23.432 15.887  1.00 49.00  ? 83  GLU   C N   1 
ATOM   2066 C CA  . GLU   C 1 84 ? 10.184  -23.289 17.315  1.00 51.92  ? 83  GLU   C CA  1 
ATOM   2067 C C   . GLU   C 1 84 ? 11.320  -22.490 17.918  1.00 52.19  ? 83  GLU   C C   1 
ATOM   2068 O O   . GLU   C 1 84 ? 11.062  -21.634 18.760  1.00 56.77  ? 83  GLU   C O   1 
ATOM   2069 C CB  . GLU   C 1 84 ? 10.032  -24.616 18.055  1.00 49.81  ? 83  GLU   C CB  1 
ATOM   2070 C CG  . GLU   C 1 84 ? 8.734   -25.313 17.672  1.00 51.89  ? 83  GLU   C CG  1 
ATOM   2071 C CD  . GLU   C 1 84 ? 8.620   -26.767 18.063  1.00 61.17  ? 83  GLU   C CD  1 
ATOM   2072 O OE1 . GLU   C 1 84 ? 9.596   -27.333 18.585  1.00 59.73  ? 83  GLU   C OE1 1 
ATOM   2073 O OE2 . GLU   C 1 84 ? 7.534   -27.337 17.828  1.00 68.57  ? 83  GLU   C OE2 1 
ATOM   2074 N N   . ILE   C 1 85 ? 12.550  -22.767 17.457  1.00 47.67  ? 84  ILE   C N   1 
ATOM   2075 C CA  . ILE   C 1 85 ? 13.723  -22.235 18.131  1.00 46.84  ? 84  ILE   C CA  1 
ATOM   2076 C C   . ILE   C 1 85 ? 13.832  -20.734 17.874  1.00 46.57  ? 84  ILE   C C   1 
ATOM   2077 O O   . ILE   C 1 85 ? 14.215  -20.007 18.775  1.00 46.17  ? 84  ILE   C O   1 
ATOM   2078 C CB  . ILE   C 1 85 ? 15.017  -23.027 17.846  1.00 43.19  ? 84  ILE   C CB  1 
ATOM   2079 C CG1 . ILE   C 1 85 ? 16.097  -22.664 18.869  1.00 43.78  ? 84  ILE   C CG1 1 
ATOM   2080 C CG2 . ILE   C 1 85 ? 15.504  -22.872 16.399  1.00 41.11  ? 84  ILE   C CG2 1 
ATOM   2081 C CD1 . ILE   C 1 85 ? 17.385  -23.475 18.790  1.00 45.05  ? 84  ILE   C CD1 1 
ATOM   2082 N N   . GLN   C 1 86 ? 13.428  -20.299 16.669  1.00 56.98  ? 85  GLN   C N   1 
ATOM   2083 C CA  . GLN   C 1 86 ? 13.317  -18.904 16.241  1.00 56.70  ? 85  GLN   C CA  1 
ATOM   2084 C C   . GLN   C 1 86 ? 12.145  -18.200 16.924  1.00 51.48  ? 85  GLN   C C   1 
ATOM   2085 O O   . GLN   C 1 86 ? 12.276  -17.064 17.353  1.00 50.42  ? 85  GLN   C O   1 
ATOM   2086 C CB  . GLN   C 1 86 ? 13.124  -18.864 14.719  1.00 56.47  ? 85  GLN   C CB  1 
ATOM   2087 C CG  . GLN   C 1 86 ? 13.281  -17.496 14.063  1.00 52.98  ? 85  GLN   C CG  1 
ATOM   2088 C CD  . GLN   C 1 86 ? 13.983  -17.520 12.711  1.00 61.70  ? 85  GLN   C CD  1 
ATOM   2089 O OE1 . GLN   C 1 86 ? 13.691  -18.327 11.812  1.00 54.58  ? 85  GLN   C OE1 1 
ATOM   2090 N NE2 . GLN   C 1 86 ? 14.943  -16.616 12.549  1.00 56.45  ? 85  GLN   C NE2 1 
ATOM   2091 N N   . ASN   C 1 87 ? 11.005  -18.887 17.048  1.00 57.48  ? 86  ASN   C N   1 
ATOM   2092 C CA  . ASN   C 1 87 ? 9.718   -18.206 17.147  1.00 59.89  ? 86  ASN   C CA  1 
ATOM   2093 C C   . ASN   C 1 87 ? 9.035   -18.464 18.493  1.00 64.79  ? 86  ASN   C C   1 
ATOM   2094 O O   . ASN   C 1 87 ? 8.250   -17.639 18.944  1.00 68.75  ? 86  ASN   C O   1 
ATOM   2095 C CB  . ASN   C 1 87 ? 8.851   -18.475 15.915  1.00 53.65  ? 86  ASN   C CB  1 
ATOM   2096 C CG  . ASN   C 1 87 ? 9.415   -17.829 14.664  1.00 53.52  ? 86  ASN   C CG  1 
ATOM   2097 O OD1 . ASN   C 1 87 ? 9.714   -16.629 14.688  1.00 62.16  ? 86  ASN   C OD1 1 
ATOM   2098 N ND2 . ASN   C 1 87 ? 9.585   -18.574 13.574  1.00 38.22  ? 86  ASN   C ND2 1 
ATOM   2099 N N   . ASN   C 1 88 ? 9.337   -19.598 19.137  1.00 64.50  ? 87  ASN   C N   1 
ATOM   2100 C CA  . ASN   C 1 88 ? 8.621   -20.018 20.334  1.00 61.64  ? 87  ASN   C CA  1 
ATOM   2101 C C   . ASN   C 1 88 ? 9.576   -20.802 21.245  1.00 64.10  ? 87  ASN   C C   1 
ATOM   2102 O O   . ASN   C 1 88 ? 9.260   -21.902 21.704  1.00 75.84  ? 87  ASN   C O   1 
ATOM   2103 C CB  . ASN   C 1 88 ? 7.380   -20.805 19.912  1.00 68.05  ? 87  ASN   C CB  1 
ATOM   2104 C CG  . ASN   C 1 88 ? 6.401   -21.068 21.030  1.00 79.23  ? 87  ASN   C CG  1 
ATOM   2105 O OD1 . ASN   C 1 88 ? 6.489   -20.444 22.094  1.00 87.83  ? 87  ASN   C OD1 1 
ATOM   2106 N ND2 . ASN   C 1 88 ? 5.459   -21.977 20.806  1.00 82.04  ? 87  ASN   C ND2 1 
ATOM   2107 N N   . PRO   C 1 89 ? 10.793  -20.295 21.540  1.00 53.44  ? 88  PRO   C N   1 
ATOM   2108 C CA  . PRO   C 1 89 ? 11.833  -21.146 22.116  1.00 57.69  ? 88  PRO   C CA  1 
ATOM   2109 C C   . PRO   C 1 89 ? 11.662  -21.581 23.572  1.00 60.88  ? 88  PRO   C C   1 
ATOM   2110 O O   . PRO   C 1 89 ? 12.461  -22.368 24.078  1.00 59.33  ? 88  PRO   C O   1 
ATOM   2111 C CB  . PRO   C 1 89 ? 13.106  -20.301 21.885  1.00 53.76  ? 88  PRO   C CB  1 
ATOM   2112 C CG  . PRO   C 1 89 ? 12.610  -18.870 21.991  1.00 57.58  ? 88  PRO   C CG  1 
ATOM   2113 C CD  . PRO   C 1 89 ? 11.230  -18.905 21.342  1.00 52.89  ? 88  PRO   C CD  1 
ATOM   2114 N N   . HIS   C 1 90 ? 10.634  -21.063 24.256  1.00 68.28  ? 89  HIS   C N   1 
ATOM   2115 C CA  . HIS   C 1 90 ? 10.523  -21.304 25.688  1.00 63.26  ? 89  HIS   C CA  1 
ATOM   2116 C C   . HIS   C 1 90 ? 9.106   -21.719 26.056  1.00 58.60  ? 89  HIS   C C   1 
ATOM   2117 O O   . HIS   C 1 90 ? 8.692   -21.505 27.185  1.00 67.97  ? 89  HIS   C O   1 
ATOM   2118 C CB  . HIS   C 1 90 ? 10.956  -20.079 26.503  1.00 61.37  ? 89  HIS   C CB  1 
ATOM   2119 C CG  . HIS   C 1 90 ? 12.303  -19.505 26.170  1.00 66.52  ? 89  HIS   C CG  1 
ATOM   2120 N ND1 . HIS   C 1 90 ? 12.491  -18.151 25.969  1.00 65.40  ? 89  HIS   C ND1 1 
ATOM   2121 C CD2 . HIS   C 1 90 ? 13.513  -20.065 25.999  1.00 63.65  ? 89  HIS   C CD2 1 
ATOM   2122 C CE1 . HIS   C 1 90 ? 13.770  -17.906 25.694  1.00 61.64  ? 89  HIS   C CE1 1 
ATOM   2123 N NE2 . HIS   C 1 90 ? 14.409  -19.053 25.712  1.00 63.42  ? 89  HIS   C NE2 1 
ATOM   2124 N N   . ALA   C 1 91 ? 8.373   -22.316 25.111  1.00 65.22  ? 90  ALA   C N   1 
ATOM   2125 C CA  . ALA   C 1 91 ? 7.047   -22.871 25.380  1.00 72.88  ? 90  ALA   C CA  1 
ATOM   2126 C C   . ALA   C 1 91 ? 7.149   -24.305 25.910  1.00 77.96  ? 90  ALA   C C   1 
ATOM   2127 O O   . ALA   C 1 91 ? 8.141   -24.993 25.663  1.00 75.21  ? 90  ALA   C O   1 
ATOM   2128 C CB  . ALA   C 1 91 ? 6.177   -22.791 24.139  1.00 67.56  ? 90  ALA   C CB  1 
ATOM   2129 N N   . SER   C 1 92 ? 6.090   -24.763 26.601  1.00 88.66  ? 91  SER   C N   1 
ATOM   2130 C CA  . SER   C 1 92 ? 6.143   -25.920 27.494  1.00 95.68  ? 91  SER   C CA  1 
ATOM   2131 C C   . SER   C 1 92 ? 6.112   -27.270 26.766  1.00 90.13  ? 91  SER   C C   1 
ATOM   2132 O O   . SER   C 1 92 ? 6.699   -28.237 27.248  1.00 84.27  ? 91  SER   C O   1 
ATOM   2133 C CB  . SER   C 1 92 ? 5.093   -25.840 28.595  1.00 94.39  ? 91  SER   C CB  1 
ATOM   2134 O OG  . SER   C 1 92 ? 5.520   -25.026 29.681  1.00 88.00  ? 91  SER   C OG  1 
ATOM   2135 N N   . TYR   C 1 93 ? 5.401   -27.352 25.633  1.00 86.24  ? 92  TYR   C N   1 
ATOM   2136 C CA  . TYR   C 1 93 ? 5.283   -28.586 24.866  1.00 85.90  ? 92  TYR   C CA  1 
ATOM   2137 C C   . TYR   C 1 93 ? 5.006   -29.777 25.816  1.00 93.47  ? 92  TYR   C C   1 
ATOM   2138 O O   . TYR   C 1 93 ? 4.156   -30.675 25.557  1.00 87.55  ? 92  TYR   C O   1 
ATOM   2139 C CB  . TYR   C 1 93 ? 6.545   -28.777 24.017  1.00 79.01  ? 92  TYR   C CB  1 
ATOM   2140 C CG  . TYR   C 1 93 ? 6.882   -27.621 23.081  1.00 78.26  ? 92  TYR   C CG  1 
ATOM   2141 C CD1 . TYR   C 1 93 ? 6.374   -27.568 21.783  1.00 75.06  ? 92  TYR   C CD1 1 
ATOM   2142 C CD2 . TYR   C 1 93 ? 7.725   -26.587 23.484  1.00 77.27  ? 92  TYR   C CD2 1 
ATOM   2143 C CE1 . TYR   C 1 93 ? 6.681   -26.525 20.920  1.00 70.02  ? 92  TYR   C CE1 1 
ATOM   2144 C CE2 . TYR   C 1 93 ? 8.035   -25.535 22.632  1.00 68.81  ? 92  TYR   C CE2 1 
ATOM   2145 C CZ  . TYR   C 1 93 ? 7.512   -25.505 21.349  1.00 67.97  ? 92  TYR   C CZ  1 
ATOM   2146 O OH  . TYR   C 1 93 ? 7.798   -24.466 20.513  1.00 67.30  ? 92  TYR   C OH  1 
HETATM 2147 S S   . SO4   D 2 .  ? 0.547   -33.552 1.982   1.00 104.30 ? 101 SO4   A S   1 
HETATM 2148 O O1  . SO4   D 2 .  ? 1.561   -34.353 1.337   1.00 96.71  ? 101 SO4   A O1  1 
HETATM 2149 O O2  . SO4   D 2 .  ? -0.199  -32.835 0.981   1.00 106.65 ? 101 SO4   A O2  1 
HETATM 2150 O O3  . SO4   D 2 .  ? -0.345  -34.397 2.735   1.00 107.82 ? 101 SO4   A O3  1 
HETATM 2151 O O4  . SO4   D 2 .  ? 1.165   -32.619 2.878   1.00 95.03  ? 101 SO4   A O4  1 
HETATM 2152 S S   . SO4   E 2 .  ? -9.974  -24.698 1.027   1.00 123.07 ? 102 SO4   A S   1 
HETATM 2153 O O1  . SO4   E 2 .  ? -10.107 -24.834 -0.403  1.00 121.91 ? 102 SO4   A O1  1 
HETATM 2154 O O2  . SO4   E 2 .  ? -10.765 -23.582 1.478   1.00 113.83 ? 102 SO4   A O2  1 
HETATM 2155 O O3  . SO4   E 2 .  ? -10.428 -25.902 1.673   1.00 118.13 ? 102 SO4   A O3  1 
HETATM 2156 O O4  . SO4   E 2 .  ? -8.594  -24.472 1.359   1.00 119.87 ? 102 SO4   A O4  1 
HETATM 2157 C C1  . EDO   F 3 .  ? 14.311  -19.135 -8.066  1.00 70.86  ? 103 EDO   A C1  1 
HETATM 2158 O O1  . EDO   F 3 .  ? 14.491  -18.886 -6.679  1.00 63.89  ? 103 EDO   A O1  1 
HETATM 2159 C C2  . EDO   F 3 .  ? 12.883  -19.327 -8.443  1.00 64.26  ? 103 EDO   A C2  1 
HETATM 2160 O O2  . EDO   F 3 .  ? 12.123  -18.140 -8.268  1.00 56.68  ? 103 EDO   A O2  1 
HETATM 2161 S S   . SO4   G 2 .  ? 8.533   -29.393 5.700   1.00 92.69  ? 104 SO4   A S   1 
HETATM 2162 O O1  . SO4   G 2 .  ? 9.275   -29.424 4.466   1.00 84.07  ? 104 SO4   A O1  1 
HETATM 2163 O O2  . SO4   G 2 .  ? 7.552   -30.448 5.699   1.00 98.60  ? 104 SO4   A O2  1 
HETATM 2164 O O3  . SO4   G 2 .  ? 9.433   -29.575 6.816   1.00 78.41  ? 104 SO4   A O3  1 
HETATM 2165 O O4  . SO4   G 2 .  ? 7.855   -28.129 5.813   1.00 106.25 ? 104 SO4   A O4  1 
HETATM 2166 S S   . SO4   H 2 .  ? 7.771   -8.106  -24.725 1.00 82.60  ? 101 SO4   B S   1 
HETATM 2167 O O1  . SO4   H 2 .  ? 8.266   -8.547  -26.005 1.00 60.79  ? 101 SO4   B O1  1 
HETATM 2168 O O2  . SO4   H 2 .  ? 6.637   -7.240  -24.922 1.00 83.28  ? 101 SO4   B O2  1 
HETATM 2169 O O3  . SO4   H 2 .  ? 7.367   -9.238  -23.930 1.00 68.27  ? 101 SO4   B O3  1 
HETATM 2170 O O4  . SO4   H 2 .  ? 8.805   -7.374  -24.038 1.00 88.59  ? 101 SO4   B O4  1 
HETATM 2171 S S   . SO4   I 2 .  ? 14.339  -27.377 -26.523 1.00 85.92  ? 102 SO4   B S   1 
HETATM 2172 O O1  . SO4   I 2 .  ? 15.302  -27.012 -25.509 1.00 80.38  ? 102 SO4   B O1  1 
HETATM 2173 O O2  . SO4   I 2 .  ? 15.005  -28.091 -27.581 1.00 96.21  ? 102 SO4   B O2  1 
HETATM 2174 O O3  . SO4   I 2 .  ? 13.311  -28.217 -25.965 1.00 80.11  ? 102 SO4   B O3  1 
HETATM 2175 O O4  . SO4   I 2 .  ? 13.735  -26.185 -27.058 1.00 98.05  ? 102 SO4   B O4  1 
HETATM 2176 N N1  . A1H9V J 4 .  ? 17.099  -15.406 -24.992 0.71 52.30  ? 103 A1H9V B N1  1 
HETATM 2177 N N3  . A1H9V J 4 .  ? 20.783  -16.721 -22.722 0.71 59.54  ? 103 A1H9V B N3  1 
HETATM 2178 C C4  . A1H9V J 4 .  ? 18.898  -16.503 -21.780 0.71 54.90  ? 103 A1H9V B C4  1 
HETATM 2179 C C5  . A1H9V J 4 .  ? 20.075  -15.954 -23.552 0.71 53.08  ? 103 A1H9V B C5  1 
HETATM 2180 C C1  . A1H9V J 4 .  ? 16.694  -14.374 -25.945 0.71 54.07  ? 103 A1H9V B C1  1 
HETATM 2181 C C2  . A1H9V J 4 .  ? 16.313  -16.640 -25.035 0.71 51.57  ? 103 A1H9V B C2  1 
HETATM 2182 C C3  . A1H9V J 4 .  ? 18.842  -15.783 -22.977 0.71 53.86  ? 103 A1H9V B C3  1 
HETATM 2183 N N2  . A1H9V J 4 .  ? 20.084  -17.071 -21.622 0.71 62.32  ? 103 A1H9V B N2  1 
HETATM 2184 O O1  . A1H9V J 4 .  ? 17.943  -13.515 -23.715 0.71 47.24  ? 103 A1H9V B O1  1 
HETATM 2185 O O2  . A1H9V J 4 .  ? 16.394  -15.155 -22.668 0.71 51.56  ? 103 A1H9V B O2  1 
HETATM 2186 S S1  . A1H9V J 4 .  ? 17.489  -14.855 -23.535 0.71 52.69  ? 103 A1H9V B S1  1 
HETATM 2187 C C1  . EDO   K 3 .  ? 16.310  -35.822 16.536  1.00 59.71  ? 101 EDO   C C1  1 
HETATM 2188 O O1  . EDO   K 3 .  ? 15.485  -36.937 16.207  1.00 60.94  ? 101 EDO   C O1  1 
HETATM 2189 C C2  . EDO   K 3 .  ? 15.785  -34.984 17.640  1.00 54.68  ? 101 EDO   C C2  1 
HETATM 2190 O O2  . EDO   K 3 .  ? 14.943  -35.756 18.471  1.00 56.28  ? 101 EDO   C O2  1 
HETATM 2191 S S   . SO4   L 2 .  ? 28.397  -37.231 11.696  1.00 141.02 ? 102 SO4   C S   1 
HETATM 2192 O O1  . SO4   L 2 .  ? 28.122  -35.948 11.096  1.00 144.41 ? 102 SO4   C O1  1 
HETATM 2193 O O2  . SO4   L 2 .  ? 27.820  -38.272 10.888  1.00 126.64 ? 102 SO4   C O2  1 
HETATM 2194 O O3  . SO4   L 2 .  ? 29.822  -37.417 11.791  1.00 138.57 ? 102 SO4   C O3  1 
HETATM 2195 O O4  . SO4   L 2 .  ? 27.827  -37.284 13.013  1.00 143.84 ? 102 SO4   C O4  1 
HETATM 2196 O O   . HOH   M 5 .  ? -5.785  -12.933 -16.575 1.00 53.80  ? 201 HOH   A O   1 
HETATM 2197 O O   . HOH   M 5 .  ? 10.445  -5.852  -4.808  1.00 41.30  ? 202 HOH   A O   1 
HETATM 2198 O O   . HOH   M 5 .  ? 4.200   -8.285  0.843   1.00 35.13  ? 203 HOH   A O   1 
HETATM 2199 O O   . HOH   M 5 .  ? 4.504   3.377   -5.995  1.00 63.61  ? 204 HOH   A O   1 
HETATM 2200 O O   . HOH   M 5 .  ? 8.586   -22.205 -9.601  1.00 57.29  ? 205 HOH   A O   1 
HETATM 2201 O O   . HOH   M 5 .  ? 9.409   -18.312 9.998   1.00 46.32  ? 206 HOH   A O   1 
HETATM 2202 O O   . HOH   M 5 .  ? 11.092  -12.334 6.086   1.00 46.11  ? 207 HOH   A O   1 
HETATM 2203 O O   . HOH   M 5 .  ? 0.631   -10.951 -15.421 1.00 63.19  ? 208 HOH   A O   1 
HETATM 2204 O O   . HOH   M 5 .  ? -6.262  -16.642 -10.436 1.00 31.61  ? 209 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? 5.271   -28.813 6.821   1.00 48.12  ? 210 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? -5.441  -19.370 -5.548  1.00 65.75  ? 211 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 10.650  -12.219 -5.856  1.00 43.00  ? 212 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? -6.335  -16.327 -8.092  1.00 20.63  ? 213 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? 6.877   -10.766 -12.070 1.00 67.61  ? 214 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? 14.920  -24.155 2.120   1.00 62.82  ? 215 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? -8.100  -16.382 -1.121  1.00 9.50   ? 216 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? 10.393  -29.455 2.178   1.00 55.30  ? 217 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? -8.630  -16.566 3.526   1.00 27.29  ? 218 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? -4.123  -30.251 -3.603  1.00 71.85  ? 219 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? 15.429  -11.819 -4.574  1.00 56.70  ? 220 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? 2.113   -24.817 -9.915  1.00 50.26  ? 221 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? 2.513   -10.162 -13.271 1.00 79.25  ? 222 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? 12.677  -8.698  -7.479  1.00 40.84  ? 223 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? -9.894  -16.178 10.363  1.00 46.73  ? 224 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 15.469  -11.408 -17.099 1.00 52.36  ? 225 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 16.961  -17.935 -9.669  1.00 51.65  ? 226 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 0.033   -23.710 9.499   1.00 55.18  ? 227 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? -0.139  -33.146 5.098   1.00 60.61  ? 228 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 0.830   -10.732 11.543  1.00 49.33  ? 229 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? -7.227  -20.784 -5.033  1.00 144.29 ? 230 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 12.586  -14.938 -12.198 1.00 60.97  ? 231 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 10.566  -5.168  -7.822  1.00 35.85  ? 232 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 4.463   -8.146  3.755   1.00 47.46  ? 233 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 2.873   -29.434 -0.652  1.00 37.46  ? 234 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? 3.432   -34.726 3.246   1.00 68.30  ? 235 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 12.673  -14.116 -8.156  1.00 42.29  ? 236 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 8.536   -31.872 3.562   1.00 72.28  ? 237 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 3.749   -3.247  -3.037  1.00 37.87  ? 238 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 16.645  -12.758 1.548   1.00 25.73  ? 239 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 9.458   -13.136 10.408  1.00 49.03  ? 240 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? -2.317  -22.087 -0.614  1.00 33.01  ? 241 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? -4.452  -21.013 6.002   1.00 36.76  ? 242 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 19.438  -15.496 7.237   1.00 41.71  ? 243 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 2.328   -24.984 -6.215  1.00 45.34  ? 244 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 10.361  -23.376 10.011  1.00 41.76  ? 245 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? -3.165  2.988   -1.677  1.00 61.71  ? 246 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 12.980  -11.721 -4.222  1.00 31.90  ? 247 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 0.106   -17.129 -19.481 1.00 62.22  ? 248 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 19.900  -20.781 -9.517  1.00 58.42  ? 249 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? -2.274  -11.373 11.323  1.00 61.12  ? 250 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? -8.717  -16.633 6.227   1.00 38.22  ? 251 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 6.948   -16.171 -14.887 1.00 43.28  ? 252 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? 1.485   -4.291  -10.574 1.00 53.27  ? 253 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? -6.359  -26.842 3.221   1.00 47.11  ? 254 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 7.720   -17.350 8.587   1.00 48.85  ? 255 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? -1.020  -20.974 7.125   1.00 36.70  ? 256 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 10.594  -7.801  0.417   1.00 38.23  ? 257 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? 11.462  -12.273 11.849  1.00 49.88  ? 258 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 13.508  -15.725 -9.191  1.00 36.59  ? 259 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 9.598   -6.121  -2.328  1.00 45.05  ? 260 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 8.635   -8.905  8.860   1.00 40.14  ? 261 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? -4.999  -9.737  6.512   1.00 62.42  ? 262 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 8.460   -9.377  -13.731 1.00 27.93  ? 263 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 8.801   -18.321 -11.067 1.00 33.70  ? 264 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -0.655  -21.686 9.903   1.00 40.60  ? 265 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 9.114   -20.351 -18.332 1.00 54.65  ? 266 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? -3.218  -29.354 7.894   1.00 48.70  ? 267 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -8.322  -16.472 1.308   1.00 13.08  ? 268 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? -7.477  -11.089 -7.925  1.00 30.33  ? 269 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 6.026   -6.465  0.419   1.00 61.61  ? 270 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? -6.776  -11.277 -11.052 1.00 42.86  ? 271 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 21.811  -16.356 -0.303  1.00 39.31  ? 272 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? -5.414  -12.612 6.818   1.00 58.43  ? 273 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 11.229  -28.744 -3.381  1.00 65.06  ? 274 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? -7.105  -12.666 5.468   1.00 57.68  ? 275 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 11.036  -16.741 -14.778 1.00 44.36  ? 276 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 2.655   -24.858 -3.173  1.00 39.11  ? 277 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? -6.650  -22.977 -6.882  1.00 57.22  ? 278 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? 8.413   -16.392 -13.134 1.00 51.30  ? 279 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 6.551   -17.392 10.794  1.00 39.16  ? 280 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? 7.575   -7.621  1.512   1.00 34.84  ? 281 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? -7.331  -14.172 -8.694  1.00 69.65  ? 282 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? -4.332  -26.662 6.672   1.00 64.27  ? 283 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? -4.139  -7.158  -10.935 1.00 37.59  ? 284 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 2.405   -6.153  5.305   1.00 50.83  ? 285 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 8.624   -27.719 -7.918  1.00 59.93  ? 286 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -1.444  -7.011  11.704  1.00 54.73  ? 287 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? -8.782  -19.613 -3.420  1.00 29.80  ? 288 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? -10.721 -12.980 -2.582  1.00 109.78 ? 289 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? 1.908   -29.015 12.263  1.00 66.81  ? 290 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 20.951  -16.201 -3.191  1.00 37.62  ? 291 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? -11.399 -16.176 -3.589  1.00 51.38  ? 292 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? -4.426  -8.064  10.552  1.00 52.83  ? 293 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? -9.734  -20.073 1.445   1.00 37.13  ? 294 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? -9.263  -20.067 -1.103  1.00 32.99  ? 295 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? 6.014   -30.092 -2.776  1.00 73.46  ? 296 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? 8.401   -18.098 -15.197 1.00 101.35 ? 297 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -6.546  -22.221 5.528   1.00 67.09  ? 298 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 2.001   -23.887 15.657  1.00 71.32  ? 299 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? -7.519  -18.716 7.758   1.00 60.02  ? 300 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -12.083 -28.709 -0.410  1.00 106.65 ? 301 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 14.413  -29.009 -2.066  1.00 67.69  ? 302 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? 11.080  -0.633  -3.948  1.00 40.31  ? 303 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 7.056   -1.766  0.966   1.00 55.26  ? 304 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 4.558   -9.107  -11.228 1.00 68.99  ? 305 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 7.621   -7.705  4.249   1.00 37.48  ? 306 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? -5.567  -20.585 -7.847  1.00 45.52  ? 307 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 4.285   -3.146  2.412   1.00 70.51  ? 308 HOH   A O   1 
HETATM 2304 O O   . HOH   N 5 .  ? 25.517  -5.534  -33.006 1.00 55.98  ? 201 HOH   B O   1 
HETATM 2305 O O   . HOH   N 5 .  ? 30.026  -19.354 -40.514 1.00 50.35  ? 202 HOH   B O   1 
HETATM 2306 O O   . HOH   N 5 .  ? 12.940  -4.015  -41.069 1.00 39.57  ? 203 HOH   B O   1 
HETATM 2307 O O   . HOH   N 5 .  ? 27.392  -8.533  -28.611 1.00 47.68  ? 204 HOH   B O   1 
HETATM 2308 O O   . HOH   N 5 .  ? 10.205  -19.830 -42.536 1.00 129.77 ? 205 HOH   B O   1 
HETATM 2309 O O   . HOH   N 5 .  ? 30.924  -7.734  -29.257 1.00 45.62  ? 206 HOH   B O   1 
HETATM 2310 O O   . HOH   N 5 .  ? 11.137  -22.631 -32.285 1.00 68.84  ? 207 HOH   B O   1 
HETATM 2311 O O   . HOH   N 5 .  ? 32.009  -18.113 -41.680 1.00 72.61  ? 208 HOH   B O   1 
HETATM 2312 O O   . HOH   N 5 .  ? 7.481   -9.172  -21.580 1.00 52.92  ? 209 HOH   B O   1 
HETATM 2313 O O   . HOH   N 5 .  ? 25.939  -22.871 -30.960 1.00 58.76  ? 210 HOH   B O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 19.529  -3.268  -23.374 1.00 90.33  ? 211 HOH   B O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 11.073  -29.173 -25.891 1.00 50.52  ? 212 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 20.220  -26.915 -36.256 1.00 48.32  ? 213 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 13.474  -22.306 -20.518 1.00 37.08  ? 214 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 17.441  -8.056  -20.364 1.00 40.79  ? 215 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 26.850  -18.473 -25.335 1.00 54.78  ? 216 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 10.876  -15.911 -44.042 1.00 56.27  ? 217 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 24.715  -5.375  -29.945 1.00 53.50  ? 218 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 25.619  -6.406  -35.276 1.00 77.28  ? 219 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 20.333  -26.384 -30.291 1.00 67.07  ? 220 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 20.124  -26.326 -33.633 1.00 40.53  ? 221 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 22.645  -28.550 -28.931 1.00 56.97  ? 222 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 20.842  -10.551 -42.328 1.00 36.94  ? 223 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 10.771  -19.050 -33.069 1.00 37.36  ? 224 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 14.189  -6.494  -40.836 1.00 40.14  ? 225 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 8.077   -26.894 -37.678 1.00 73.02  ? 226 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 5.950   -12.060 -25.884 1.00 33.20  ? 227 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 21.674  -24.477 -29.136 1.00 60.41  ? 228 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 16.729  -19.028 -28.479 1.00 29.84  ? 229 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 39.298  -12.284 -38.975 1.00 56.53  ? 230 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 25.589  -0.746  -28.859 1.00 49.12  ? 231 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 17.847  -19.882 -41.835 1.00 51.76  ? 232 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 23.267  -4.319  -36.415 1.00 49.68  ? 233 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 17.748  -23.183 -20.545 1.00 41.32  ? 234 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 21.584  3.268   -32.591 1.00 43.76  ? 235 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 17.561  4.613   -34.722 1.00 59.99  ? 236 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 14.277  -24.378 -40.222 1.00 39.31  ? 237 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 24.715  -8.176  -42.200 1.00 49.90  ? 238 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 23.190  -3.487  -28.617 1.00 49.06  ? 239 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 27.154  -11.100 -28.271 1.00 104.73 ? 240 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 24.300  -2.179  -36.055 1.00 53.42  ? 241 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 17.936  -15.801 -45.338 1.00 43.99  ? 242 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 17.831  -0.895  -38.269 1.00 49.80  ? 243 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 14.534  -8.576  -43.110 1.00 80.48  ? 244 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 23.630  -11.583 -21.652 1.00 46.60  ? 245 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 4.411   -19.245 -30.873 1.00 50.48  ? 246 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 17.542  -1.140  -24.880 1.00 64.54  ? 247 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 8.084   -9.128  -16.425 1.00 24.92  ? 248 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 10.468  -11.950 -37.334 1.00 87.23  ? 249 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 31.354  -12.583 -37.791 1.00 66.66  ? 250 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 1.856   -13.437 -28.234 1.00 63.27  ? 251 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 7.173   -19.533 -34.339 1.00 36.92  ? 252 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 17.530  -10.050 -43.489 1.00 49.48  ? 253 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 7.376   -19.233 -31.585 1.00 43.85  ? 254 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 6.453   -6.577  -33.195 1.00 132.36 ? 255 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 17.797  -26.864 -28.861 1.00 60.43  ? 256 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 7.708   -20.777 -26.648 1.00 60.92  ? 257 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 11.921  -20.951 -19.658 1.00 64.63  ? 258 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 28.332  -24.780 -35.058 1.00 37.39  ? 259 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 9.300   -6.085  -40.358 1.00 55.37  ? 260 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 22.895  -7.464  -21.053 1.00 64.27  ? 261 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 32.334  -22.122 -37.566 1.00 40.01  ? 262 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 21.899  -13.620 -42.409 1.00 57.51  ? 263 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 2.850   -7.942  -27.346 1.00 49.43  ? 264 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 24.426  -17.301 -23.015 1.00 53.11  ? 265 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 6.524   -20.918 -29.497 1.00 67.51  ? 266 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 25.050  -26.476 -28.273 1.00 58.79  ? 267 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 19.668  3.381   -33.210 1.00 54.77  ? 268 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 8.662   -3.413  -28.833 1.00 60.22  ? 269 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 17.673  -2.336  -22.143 1.00 69.68  ? 270 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 36.756  -23.932 -28.951 1.00 59.82  ? 271 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 5.151   -19.959 -25.557 1.00 49.49  ? 272 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 15.155  -21.567 -41.703 1.00 59.38  ? 273 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 9.432   -20.528 -32.890 1.00 52.26  ? 274 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 7.581   -9.329  -18.910 1.00 31.83  ? 275 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 19.553  -8.961  -42.904 1.00 45.70  ? 276 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 9.361   -22.537 -18.770 1.00 60.42  ? 277 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 41.352  -11.270 -36.998 1.00 52.50  ? 278 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 39.631  -19.158 -40.047 1.00 51.60  ? 279 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 11.340  -3.799  -20.962 1.00 51.98  ? 280 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 17.167  5.398   -27.564 1.00 52.26  ? 281 HOH   B O   1 
HETATM 2385 O O   . HOH   O 5 .  ? 12.349  -28.023 28.544  1.00 48.87  ? 201 HOH   C O   1 
HETATM 2386 O O   . HOH   O 5 .  ? 27.564  -36.131 25.069  1.00 52.53  ? 202 HOH   C O   1 
HETATM 2387 O O   . HOH   O 5 .  ? 27.273  -15.273 12.542  1.00 51.47  ? 203 HOH   C O   1 
HETATM 2388 O O   . HOH   O 5 .  ? 30.571  -31.092 18.465  1.00 38.68  ? 204 HOH   C O   1 
HETATM 2389 O O   . HOH   O 5 .  ? 26.175  -39.038 12.277  1.00 56.33  ? 205 HOH   C O   1 
HETATM 2390 O O   . HOH   O 5 .  ? 16.923  -38.847 11.773  1.00 60.50  ? 206 HOH   C O   1 
HETATM 2391 O O   . HOH   O 5 .  ? 6.836   -31.217 11.819  1.00 54.13  ? 207 HOH   C O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 9.046   -36.465 20.374  1.00 63.47  ? 208 HOH   C O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 20.350  -40.145 39.123  1.00 57.41  ? 209 HOH   C O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 22.746  -21.777 7.203   1.00 48.05  ? 210 HOH   C O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 17.153  -16.933 14.834  1.00 43.92  ? 211 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 23.040  -40.647 18.463  1.00 68.62  ? 212 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 19.614  -41.713 12.138  1.00 36.81  ? 213 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 24.944  -30.987 10.694  1.00 47.90  ? 214 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 30.164  -27.582 31.708  1.00 43.33  ? 215 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 5.952   -25.675 16.624  1.00 106.57 ? 216 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 30.542  -42.586 15.422  1.00 70.02  ? 217 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 27.326  -24.157 32.564  1.00 88.24  ? 218 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 20.389  -28.366 8.344   1.00 41.70  ? 219 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 15.813  -37.267 20.415  1.00 53.57  ? 220 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 21.489  -34.249 16.494  1.00 40.56  ? 221 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 25.803  -36.823 9.998   1.00 53.69  ? 222 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 25.066  -19.756 6.175   1.00 45.91  ? 223 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 19.238  -13.228 16.643  1.00 46.24  ? 224 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 21.663  -28.589 11.114  1.00 50.58  ? 225 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 30.219  -39.908 26.791  1.00 76.26  ? 226 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 11.980  -30.910 8.563   1.00 49.98  ? 227 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 30.067  -35.326 29.241  1.00 139.26 ? 228 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 24.937  -14.751 10.910  1.00 73.73  ? 229 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 30.241  -27.233 29.192  1.00 50.63  ? 230 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 22.411  -18.303 21.237  1.00 56.85  ? 231 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 25.862  -38.720 19.851  1.00 49.95  ? 232 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 25.581  -17.893 13.575  1.00 40.94  ? 233 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 24.764  -17.862 20.692  1.00 47.90  ? 234 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 9.150   -30.110 9.929   1.00 40.70  ? 235 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 18.547  -19.191 29.211  1.00 61.04  ? 236 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 19.809  -13.092 13.173  1.00 48.53  ? 237 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 27.995  -37.261 15.908  1.00 49.76  ? 238 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 14.580  -21.282 11.888  1.00 45.88  ? 239 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 31.218  -42.522 11.322  1.00 53.12  ? 240 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 25.382  -33.452 34.869  1.00 62.80  ? 241 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 13.102  -39.222 16.814  1.00 47.55  ? 242 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 16.808  -17.333 24.926  1.00 59.88  ? 243 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 13.770  -38.687 9.547   1.00 56.82  ? 244 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 21.382  -34.146 7.335   1.00 53.90  ? 245 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 13.357  -29.547 38.402  1.00 68.66  ? 246 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 28.820  -39.587 31.203  1.00 49.99  ? 247 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 31.461  -37.835 30.377  1.00 68.98  ? 248 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 19.035  -18.806 25.449  1.00 52.50  ? 249 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 14.588  -31.980 2.554   1.00 48.06  ? 250 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 33.392  -24.665 31.762  1.00 65.37  ? 251 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 11.636  -20.800 10.597  1.00 42.54  ? 252 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 27.628  -38.784 24.741  1.00 49.58  ? 253 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 30.518  -30.794 13.383  1.00 50.87  ? 254 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 16.119  -17.022 19.072  1.00 48.08  ? 255 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 4.151   -17.901 22.925  1.00 56.87  ? 256 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 16.655  -36.422 29.269  1.00 53.65  ? 257 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 21.996  -13.502 12.806  1.00 38.21  ? 258 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 30.565  -31.018 16.140  1.00 40.01  ? 259 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 8.821   -17.633 23.049  1.00 43.37  ? 260 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 20.975  -28.415 3.368   1.00 54.41  ? 261 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 20.243  -18.911 10.918  1.00 80.53  ? 262 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 24.036  -28.620 9.824   1.00 113.17 ? 263 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 26.414  -19.758 25.807  1.00 56.65  ? 264 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 13.089  -21.888 28.068  1.00 59.47  ? 265 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 4.188   -24.386 17.252  1.00 59.19  ? 266 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 28.574  -15.725 20.232  1.00 67.08  ? 267 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 20.493  -40.379 23.834  1.00 57.08  ? 268 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 1.862   -21.352 17.519  1.00 62.69  ? 269 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 37.386  -24.269 25.852  1.00 71.34  ? 270 HOH   C O   1 
# 
